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I want to measure the amount of lactic acid in silage samples using gas chromatography. Can I extract the silage using alcohol?
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@Yuri Freddy Peña-Rueda
thank you for your help.
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Hello. Has anyone ever measured lactic acid amounts using colorimetric methods? I measured lactic acid using this method (Taylor, 1996), but I encountered some issues. Should the control samples, which contain no lactic acid, form a color with the reagent? Additionally, the resulting standard curve was a downward-sloping linear curve; what could be the reasons for these discrepancies?
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You are welcome.
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I can fathom the idea of PK being different b/w dogs and rodents, but why would I be seeing a significantly different PK profile for the same drug tested on rats and mice?
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Dear Colleague,
I hope this message finds you well. Understanding the pharmacokinetic (PK) differences between rats and mice is essential for interpreting preclinical data and translating findings to human applications. Several factors contribute to these differences, which I detail below:
  1. Metabolic Rate:Basal Metabolic Rate: Mice generally have a higher basal metabolic rate compared to rats. This can lead to faster drug metabolism and clearance in mice, impacting drug half-life and bioavailability.
  2. Enzyme Expression:Cytochrome P450 Isoenzymes: The expression levels and activity of cytochrome P450 enzymes can differ significantly between rats and mice. These enzymes play a crucial role in the metabolism of many drugs, influencing the rate of biotransformation and the formation of metabolites. Phase II Enzymes: Differences in the expression of phase II enzymes (e.g., glucuronidation and sulfation enzymes) also contribute to variations in drug conjugation and elimination.
  3. Absorption:Gastrointestinal Differences: Variations in gastrointestinal pH, transit time, and the expression of transporters and enzymes in the gut can affect the absorption rate and extent of orally administered drugs.
  4. Distribution:Body Composition: Differences in body fat composition and tissue distribution can influence the volume of distribution (Vd) of lipophilic drugs. Rats and mice may have different Vd values, affecting drug concentration in tissues. Plasma Protein Binding: Variations in plasma protein binding between species can alter the free (active) drug concentration, impacting the drug’s pharmacodynamics and kinetics.
  5. Excretion:Renal Function: Differences in renal blood flow, glomerular filtration rate (GFR), and tubular secretion between rats and mice can affect the excretion rate of drugs and their metabolites. Biliary Excretion: Species-specific differences in biliary excretion can influence the elimination of drugs that are primarily excreted via the bile.
  6. Physiological and Anatomical Differences:Organ Size and Function: Variations in the size and function of organs involved in drug metabolism and excretion (e.g., liver, kidneys) can impact pharmacokinetic profiles. Blood-Brain Barrier: Differences in the permeability of the blood-brain barrier can affect the distribution of drugs to the central nervous system.
  7. Genetic Factors:Strain-Specific Differences: Genetic variability between different strains of rats and mice can result in differences in drug metabolism and response. It is important to consider strain-specific characteristics when comparing PK data.
  8. Experimental Conditions:Housing and Diet: Variations in housing conditions, diet, and handling can influence physiological parameters and, consequently, drug pharmacokinetics. Standardizing these conditions is crucial for minimizing variability. Administration Route and Formulation: The route of administration (e.g., oral, intravenous) and the formulation of the drug (e.g., solution, suspension) can lead to differences in absorption and bioavailability between species.
In conclusion, multiple factors, including metabolic rate, enzyme expression, absorption, distribution, excretion, physiological and anatomical differences, genetic factors, and experimental conditions, contribute to the pharmacokinetic differences observed between rats and mice. Careful consideration and control of these factors are essential for accurate interpretation and comparison of PK data across species.
Should you have any further questions or require additional assistance, please feel free to reach out.
What factors may contribute to the PK differences in rats and mice?
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I'm inducing (Repeated exposure) lung inflammation by using organic dust; I want to know how we can determine whether the mice's lungs will inflammated or not.
What are the symptoms clinical examination can be seen in the mice?
Thanks in advance
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Have you done characterization of the organic dust? For VOC's, PAH'S or metals?
I expose C67/BL6 mice with PM 2.5 and the functional parameters of the mice lungs are affected from 15th day itself. So if you have instruments to assess the lung function such as whole body plethysmography or FlexiVent analysis, you could check the same at 15th day interval and from then on every 7 days interval to check how the inflammation and lung function are being affected due to repeated exposure of organic dust particles.
Thanks
Samir
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Hi all, I will appreciate if you could direct me to a paper where I can find the stomach pH in crustaceans. I am sure it will vary between species, yet any data will be useful and much appreciated.
Thanks
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Tam Quyet Nguyen Very good picture. May I know the source of it? Thanks.
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Hello,
I would like to know how much long can I conserve serum samples in - 20°C for biochemical analysis : lipid profile (cholesterol, triglyceride...), protein profile (albumin, total protein...), enzymatic (ASAT, ALAT...), glucose .
Thank you in advance
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Answer: Prior to shipment or for a maximum of 48 hours, serum should be kept between 4 and 8°C. 7 days. Serum samples held for longer periods of time should be frozen at or below 20°C and sent to the testing facility on frozen ice packs.
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Hi folks,
I extracted BAL fluid from mice to check total and differential leukocyte counts, as well as inflammatory cytokines and chemokines, and now I'm wondering how long I can keep my samples at -80 degrees to check the same. Suggest some practical experiences or methods for a better result.
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After collecting BALF, keep it on ice and do the cytospin within 2-3 h.
If you want to collect the total cells, after collecting BALF, centrifuge it at 5000 g for 10 min in a microfuge centrifuge. The pellet can be suspended back in ice cold physiological saline for staining and visualization under microscope. All these should be done keeping the samples on ice and within 2-3 h of BALF collection. I would suggest getting it done as son as BALF gets collected!
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I have approached various companies but they aren't dealing with an Elisa kit which can measure corticosterone level in brain tissue homogenate. Can anyone suggest me such kit? Is it possible( considering sensitivity) to use a kit for brain tissue homogenate which is marketed for plasma, serum, urine, milk etc?
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Hi guys, anyone has good results with corticosterone ELISA Kit DetectX by Arbor Assays on brain tissue homogenate?
¡Cheers!
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Among various factors, the temperature is one of the most crucial factor for enzyme activity. For most of the enzyme assay, researcher use 37oC or normal room temperature as incubation temperature. If we consider the poikilothermic animals like fish, it's natural enzyme activity depends on habitat temperature and each fish (tropical, temperate, polar or cold water species) has their optimum temperature at which it grows best and we know growth is nothing but a consequence of optimum (good) metabolism.
So, is it right to use the mentioned assay temperature for enzyme activity of fish irrespective of its natural habitat?
Or,
Do the researchers need to modify the assay temperature according to optimum natural habitat temperature of fish?
Please provide your suggestions.
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We may not adopt a single temperature for fish enzymes such as 37ºC in case of human samples. It should be specific the species as fish is not a single species. Again, we need to find optimum temp for each of the enzymes as well. For convenience, we can select a constant temperature for all enzyme assays, which can be selected based on the optimum temperature for growth of that species. In the following publication, you will find an optimum range of temperature for digestive enzymes, however its quite a wide one (45-65ºC) https://scialert.net/fulltext/?doi=jfas.2017.264.272#:~:text=The%20optimum%20temperatures%20for%20both,water%20temperature%20of%20the%20swamp.
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we did plasma measurement of cho and tri. in our mouse samples, now we would like to measure direct level in the fresh tissues, does anyone know where we could do this around montreal area, or any kits that can be used for this!
thanks
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Hi Dear friend,
Along as I am working on an animal model study as C57lb/6J mice to determining the cholesterol concentration in blood serum and in the liver.
But now I am planning to extract the liver and the purpose wants to measure the cholesterol concentration. and if anybody know the procedure please recommend me or give me some idea about it.
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to detect meat produced from stressed animals suitable for human consumption?
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Please take a look at these useful PDF attachments.
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Could give me please some guidelines to know where to start? I'm looking for the metabolic pathway of resveratrol and thus find a way to see their influence on some cofactor or the same growth hormone.
There is an review to have an panorame of this topic.
Thank you
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There animal studies, some showing a increase in growth hormone or the related IGF-1, others show a decrease, so its hard to know what it will do in people, it might be biphasic, dose dependent. Here the abstracts I found:
Am J Vet Res. 2014 Aug;75(8):752-9. doi: 10.2460/ajvr.75.8.752.
Modulation of growth and immunity by dietary supplementation with resveratrol in young chickens receiving conventional vaccinations.
Zhang C1, Tian Y, Yan F, Kang X, Han R, Sun G, Zhang H.
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Abstract
OBJECTIVE:
To determine the effects of resveratrol (RES) on growth and immune status in chickens receiving conventional vaccinations.
ANIMALS:
Two hundred forty 1-day-old layer chickens.
PROCEDURES:
Chickens received conventional vaccinations throughout the study and were randomly assigned to 1 of 4 treatments in 6 replicate pens/treatment. Treatments included 1 control group (basal diet) and 3 experimental groups fed the basal diet plus 200, 400, and 800 mg of RES/kg of diet. At 40 days of age, 1 bird/pen was randomly selected to have blood and tissues collected to determine serum immunity indices; mRNA relative expression of proinflammatory cytokines in splenocytes; mRNA relative expression of nuclear transcription factor-κB, growth hormone receptor, and insulin-like growth factor-1 in hepatocytes; cell proliferation; and apoptosis.
RESULTS:
Average daily gain, antibody titers against Newcastle disease virus and avian influenza viruses H5 and H9, and insulin-like growth factor-1 expression were quadratically increased with increasing RES concentration. In hepatocytes, growth hormone receptor gene mRNA relative expression was quadratically increased and nuclear transcription factor-κB gene mRNA relative expression was linearly decreased with increasing RES concentration. In splenocytes, nterleukin-1β and tumor necrosis factor-α mRNA relative expression was linearly decreased with increasing RES concentration. Resveratrol supplementation delayed cell proliferation and reduced apoptosis in immunocytes. With increasing RES concentration, proliferation index and relative weight of the thymus, ratio of CD4+ to CD8+ cells, and CD4+ cell count were quadratically increased, and IgM concentration was linearly increased.
CONCLUSIONS AND CLINICAL RELEVANCE:
Dietary resveratrol supplementation improved growth, protected immunocytes against antigen-induced apoptosis, and upregulated immune response in chickens that received conventional vaccinations.
PMID:
25061707
DOI:
10.2460/ajvr.75.8.752
[Indexed for MEDLINE]
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Publication types, MeSH terms, Substances
Select item 24570423 2.
Poult Sci. 2014 Jan;93(1):54-62. doi: 10.3382/ps.2013-03423.
Resveratrol induces antioxidant and heat shock protein mRNA expression in response to heat stress in black-boned chickens.
Liu LL1, He JH, Xie HB, Yang YS, Li JC, Zou Y.
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Abstract
This study investigated the effects of dietary resveratrol at 0, 200, 400, or 600 mg/kg of diet on the performance, immune organ growth index, serum parameters, and expression levels of heat shock protein (Hsp) 27, Hsp70, and Hsp90 mRNA in the bursa of Fabricius, thymus, and spleen of 42-d-old female black-boned chickens exposed to heat stress at 37 ± 2°C for 15 d. The results showed that heat stress reduced daily feed intake and BW gain; decreased serum glutathione (GSH), growth hormone, and insulin-like growth factor-1 levels; and inhibited GSH peroxidase (GSH-Px), superoxide dismutase (SOD), and catalase (CAT) activities compared with birds subjected to thermo-neutral circumstances. Chickens that were fed diets supplemented with resveratrol exhibited a linear increase in feed intake and BW gain (P < 0.001); serum GSH, growth hormone, and insulin-like growth factor-1 levels (P ≤ 0.01); and GSH-Px, SOD, and CAT activities (P < 0.001) compared with chickens that were fed diets without resveratrol during heat stress. In contrast, serum malonaldehyde concentrations were decreased (P < 0.001) in the chickens fed a resveratrol-supplemented diet. Heat stress also reduced (P < 0.05) the growth index of the bursa of Fabricus and spleen; however, it had no effect on the growth index of the thymus. The growth index of the bursa of Fabricius and spleen increased (P < 0.05) upon heat stress and coincided with an increase in supplemental resveratrol levels. The expression of Hsp27, Hsp70, and Hsp90 mRNA in the bursa of Fabricius and spleen were increased (P < 0.01), but those of Hsp27 and Hsp90 mRNA in thymus were decreased (P < 0.01) under heat stress compared with no heat stress. Resveratrol attenuated the heat stress-induced overexpression of Hsp27, Hsp70, and Hsp90 mRNA in the bursa of Fabricius and spleen and increased the low expression of Hsp27 and Hsp90 mRNA in thymus upon heat stress. The results suggest that supplemental resveratrol improves growth performance and reduces oxidative stress in heat-stressed black-boned chickens by increasing serum growth hormone concentrations and modulating the expression of heat shock genes in organs of the immune system.
KEYWORDS:
antioxidant response; black-boned chicken; heat shock protein; heat stress; resveratrol
PMID:
24570423
DOI:
10.3382/ps.2013-03423
[Indexed for MEDLINE]
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FASEB J. 2013 Apr;27(4):1561-71. doi: 10.1096/fj.12-220129. Epub 2013 Jan 4.
Sirt1 inhibits the transcription factor CREB to regulate pituitary growth hormone synthesis.
Monteserin-Garcia J1, Al-Massadi O, Seoane LM, Alvarez CV, Shan B, Stalla J, Paez-Pereda M, Casanueva FF, Stalla GK, Theodoropoulou M.
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Abstract
Growth hormone (GH) is a major anabolic hormone and the primary regulator of organism growth. Its transcription is triggered by GH-releasing hormone (GHRH) through the transcription factor cAMP response element-binding protein (CREB) and by caloric intake. In contrast, the deacetylase Sirt1 is activated by caloric restriction. Therefore, the present study investigates how Sirt1 affects CREB function and GH synthesis. Sirt1 pharmacological activation with resveratrol (IC₅₀=87 μM) suppressed GHRH-induced GH secretion from rat anterior pituitary cells in vivo and in vitro, while vehicle controls showed no effect. Resveratrol's effects were abolished after knocking down Sirt1 with RNA interference, but not in control scrambled siRNA-transfected rat somatotrophs, confirming the Sirt1 specificity. Sirt1 activation and overexpression suppressed forskolin-induced CREB-Ser(133) phosphorylation, but no effect was seen with vehicle and empty plasmid controls. The deacetylase-dead mutant Sirt1 retained CREB-Ser(133) phosphorylation by keeping protein phosphatase protein phosphatase 1 activity low. Sirt1 activation suppressed glycogen synthase kinase 3 β acetylation, and a mutation on the GSK3β-Lys(205) residue mimicking a hypoacetylated form revealed increased activity. In summary, this is a novel mechanism through which Sirt1 intercepts the cAMP pathway by suppressing CREB transcriptional activation, resulting in decreased GH synthesis.
PMID:
23292070
DOI:
10.1096/fj.12-220129
[Indexed for MEDLINE]
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Carcinogenesis. 2007 Sep;28(9):1946-53. Epub 2007 Aug 3.
Resveratrol suppresses prostate cancer progression in transgenic mice.
Harper CE1, Patel BB, Wang J, Arabshahi A, Eltoum IA, Lamartiniere CA.
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Abstract
Resveratrol, a natural polyphenolic phytochemical, has been reported to act as an antioxidant and provide anticancer activities. We hypothesized that resveratrol would exert a chemopreventive effect against prostate cancer via regulation of sex steroid receptor and growth factor signaling pathways. In the current study, Transgenic Adenocarcinoma Mouse Prostate males were fed resveratrol (625 mg resveratrol per kg AIN-76A diet) or phytoestrogen-free, control diet (AIN-76A) starting at 5 weeks of age. Mechanisms of action and histopathology studies were conducted at 12 and 28 weeks of age, respectively. Resveratrol in the diet significantly reduced the incidence of poorly differentiated prostatic adenocarcinoma by 7.7-fold. In the dorsolateral prostate, resveratrol significantly inhibited cell proliferation, increased androgen receptor, estrogen receptor-beta, and insulin-like growth factor-1 receptor, and significantly decreased insulin-like growth factor (IGF)-1 and phospho-extracellular regulating kinase 1 (phospho-ERK 1). In the ventral prostate, resveratrol significantly reduced cell proliferation and phospho-ERKs 1 and 2, but did not significantly alter insulin-like growth factor-1 receptor and IGF-1. Serum total testosterone, free testosterone, estradiol, dihydrotestosterone and sex hormone-binding globulin (SHBG) concentrations and Simian Virus-40 large T antigen expression in the prostate were not altered in resveratrol-treated mice. Total resveratrol concentration in the blood serum of 12-week-old mice treated for 3 weeks with 625 mg resveratrol per kg diet was 52 +/- 18 nM. The decrease in cell proliferation and the potent growth factor, IGF-1, the down-regulation of downstream effectors, phospho-ERKs 1 and 2 and the increase in the putative tumor suppressor, estrogen receptor-beta, provide a biochemical basis for resveratrol suppressing prostate cancer development.
PMID:
17675339
DOI:
10.1093/carcin/bgm144
[Indexed for MEDLINE]
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Nutr Metab (Lond). 2010 May 10;7:40. doi: 10.1186/1743-7075-7-40.
Subchronic exposure to phytoestrogens alone and in combination with diethylstilbestrol - pituitary tumor induction in Fischer 344 rats.
Jeng YJ1, Kochukov M, Nauduri D, Kaphalia BS, Watson CS.
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Abstract
BACKGROUND:
Subchronic administration of the potent pharmaceutical estrogen diethylstilbestrol (DES) to female Fischer 344 (F344) rats induces growth of large, hemorrhagic pituitaries that progress to tumors. Phytoestrogens (dietary plant estrogens) are hypothesized to be potential tumor inhibitors in tissues prone to estrogen-induced cancers, and have been suggested as "safer" estrogen replacements. However, it is unknown if they might themselves establish or exacerbate the growth of estrogen-responsive cancers, such as in pituitary.
METHODS:
We implanted rats with silastic capsules containing 5 mg of four different phytoestrogens - either coumestrol, daidzein, genistein, or trans-resveratrol, in the presence or absence of DES. We examined pituitary and other organ weights, blood levels of prolactin (PRL) and growth hormone (GH), body weights, and pituitary tissue histology.
RESULTS:
Blood level measurements of the administered phytoestrogens confirmed successful exposure of the animals to high levels of these compounds. By themselves, no phytoestrogen increased pituitary weights or serum PRL levels after 10 weeks of treatment. DES, genistein, and resveratrol increased GH levels during this time. Phytoestrogens neither changed any wet organ weight (uterus, ovary, cervix, liver, and kidney) after 10 weeks of treatment, nor reversed the adverse effects of DES on pituitaries, GH and PRL levels, or body weight gain after 8 weeks of co-treatment. However, they did reverse the DES-induced weight increase on the ovary and cervix. Morphometric examination of pituitaries revealed that treatment with DES, either alone or in combination with phytoestrogens, caused gross structural changes that included decreases in tissue cell density, increases in vascularity, and multiple hemorrhagic areas. DES, especially in combination with phytoestrogens, caused the development of larger and more heterogeneous nuclear sizes in pituitary.
CONCLUSIONS:
High levels of phytoestrogens by themselves did not cause pituitary precancerous growth or change weights of other estrogen-sensitive organs, though when combined with DES, they counteracted the growth effects of DES on reproductive organs. In the pituitary, phytoestrogens did not reverse the effects of DES, but they did increase the sizes and size heterogeneity of nuclei. Therefore, phytoestrogens may oppose some but not all estrogen-responsive tissue abnormalities caused by DES overstimulation, and appear to exacerbate DES-induced nuclear changes.
PMID:
20459739
PMCID:
PMC2881934
DOI:
10.1186/1743-7075-7-40
Free PMC Article
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differences between alkaline phosphatase and acidic phosphates
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Forgot to mention, you may look at the list of currently recognized phosphatases at BRENDA enzyme database:
there are 109 enzyme activities under the category of phosphate hydrolase (EC 3.1.3.x), this is the complete list:
3.1.3.1 alkaline phosphatase
3.1.3.2 acid phosphatase
3.1.3.3 phosphoserine phosphatase
3.1.3.4 phosphatidate phosphatase
3.1.3.5 5'-nucleotidase
3.1.3.6 3'-nucleotidase
3.1.3.7 3'(2'),5'-bisphosphate nucleotidase
3.1.3.8 3-phytase
3.1.3.9 glucose-6-phosphatase
3.1.3.10 glucose-1-phosphatase
3.1.3.11 fructose-bisphosphatase
3.1.3.12 trehalose-phosphatase
3.1.3.13 bisphosphoglycerate phosphatase
3.1.3.14 methylphosphothioglycerate phosphatase
3.1.3.15 histidinol-phosphatase
3.1.3.16 protein-serine/threonine phosphatase
3.1.3.17 [phosphorylase] phosphatase
3.1.3.18 phosphoglycolate phosphatase
3.1.3.19 glycerol-2-phosphatase
3.1.3.20 phosphoglycerate phosphatase
3.1.3.21 glycerol-1-phosphatase
3.1.3.22 mannitol-1-phosphatase
3.1.3.23 sugar-phosphatase
3.1.3.24 sucrose-phosphate phosphatase
3.1.3.25 inositol-phosphate phosphatase
3.1.3.26 4-phytase
3.1.3.27 phosphatidylglycerophosphatase
3.1.3.28 ADP-phosphoglycerate phosphatase
3.1.3.29 N-acylneuraminate-9-phosphatase
3.1.3.30 3'-phosphoadenylylsulfate 3'-phosphatase
3.1.3.31 nucleotidase
3.1.3.32 polynucleotide 3'-phosphatase
3.1.3.33 polynucleotide 5'-phosphatase
3.1.3.34 deoxynucleotide 3'-phosphatase
3.1.3.35 thymidylate 5'-phosphatase
3.1.3.36 phosphoinositide 5-phosphatase
3.1.3.37 sedoheptulose-bisphosphatase
3.1.3.38 3-phosphoglycerate phosphatase
3.1.3.39 streptomycin-6-phosphatase
3.1.3.40 guanidinodeoxy-scyllo-inositol-4-phosphatase
3.1.3.41 4-nitrophenylphosphatase
3.1.3.42 [glycogen-synthase-D] phosphatase
3.1.3.43 [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
3.1.3.44 [acetyl-CoA carboxylase]-phosphatase
3.1.3.45 3-deoxy-manno-octulosonate-8-phosphatase
3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase
3.1.3.47 [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase
3.1.3.48 protein-tyrosine-phosphatase
3.1.3.49 [pyruvate kinase]-phosphatase
3.1.3.50 sorbitol-6-phosphatase
3.1.3.51 dolichyl-phosphatase
3.1.3.52 [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphatase
3.1.3.53 [myosin-light-chain] phosphatase
3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase
3.1.3.55 caldesmon-phosphatase
3.1.3.56 inositol-polyphosphate 5-phosphatase
3.1.3.57 inositol-1,4-bisphosphate 1-phosphatase
3.1.3.58 sugar-terminal-phosphatase
3.1.3.59 alkylacetylglycerophosphatase
3.1.3.60 phosphoenolpyruvate phosphatase
3.1.3.61 inositol-1,4,5-trisphosphate 1-phosphatase
3.1.3.62 multiple inositol-polyphosphate phosphatase
3.1.3.63 2-carboxy-D-arabinitol-1-phosphatase
3.1.3.64 phosphatidylinositol-3-phosphatase
3.1.3.65 inositol-1,3-bisphosphate 3-phosphatase
3.1.3.66 phosphatidylinositol-3,4-bisphosphate 4-phosphatase
3.1.3.67 phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
3.1.3.68 2-deoxyglucose-6-phosphatase
3.1.3.69 glucosylglycerol 3-phosphatase
3.1.3.70 mannosyl-3-phosphoglycerate phosphatase
3.1.3.71 2-phosphosulfolactate phosphatase
3.1.3.72 5-phytase
3.1.3.73 adenosylcobalamin/alpha-ribazole phosphatase
3.1.3.74 pyridoxal phosphatase
3.1.3.75 phosphoethanolamine/phosphocholine phosphatase
3.1.3.76 lipid-phosphate phosphatase
3.1.3.77 acireductone synthase
3.1.3.78 phosphatidylinositol-4,5-bisphosphate 4-phosphatase
3.1.3.79 mannosylfructose-phosphate phosphatase
3.1.3.80 2,3-bisphosphoglycerate 3-phosphatase
3.1.3.81 diacylglycerol diphosphate phosphatase
3.1.3.82 D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase
3.1.3.83 D-glycero-alpha-D-manno-heptose 1,7-bisphosphate 7-phosphatase
3.1.3.84 ADP-ribose 1''-phosphate phosphatase
3.1.3.85 glucosyl-3-phosphoglycerate phosphatase
3.1.3.86 phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase
3.1.3.87 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase
3.1.3.88 5''-phosphoribostamycin phosphatase
3.1.3.89 5'-deoxynucleotidase
3.1.3.90 maltose 6'-phosphate phosphatase
3.1.3.91 7-methylguanosine nucleotidase
3.1.3.92 kanosamine-6-phosphate phosphatase
3.1.3.93 L-galactose 1-phosphate phosphatase
3.1.3.94 D-galactose 1-phosphate phosphatase
3.1.3.95 phosphatidylinositol-3,5-bisphosphate 3-phosphatase
3.1.3.96 pseudouridine 5'-phosphatase
3.1.3.97 3',5'-nucleoside bisphosphate phosphatase
3.1.3.98 CDP-glycerol:N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol glycerophosphotransferase
3.1.3.99 IMP-specific 5'-nucleotidase
3.1.3.100 thiamine phosphate phosphatase
3.1.3.101 validoxylamine A 7'-phosphate phosphatase
3.1.3.102 FMN hydrolase
3.1.3.103 3-deoxy-D-glycero-D-galacto-nononate 9-phosphatase
3.1.3.104 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase
3.1.3.B4 phosphatidylinositol-4-phosphate phosphatase
3.1.3.B8 mannosylglucosyl-3-phosphoglycerate phosphatase
3.1.3.B9 L-galactose 1-phosphate phosphatase
3.1.3.B13 sn-2-glycerol-3-phosphate phosphatase
3.1.3.B14 archaetidylinositol phosphate phosphatase
Best wishes,
Rogelio
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I have isolated a pure compound from a medicinal plant and now want to check its activity in mice models. In this case, what samples should I to take into account from the following?:
1. crude extract of medicinal plant
2. partially purified extract(s) of medicinal plant
3. Pure (HPLC purity more than 98%) compund
I have seen some research articles which use both, crude extract and pure compounds for such animal studies. Is it needed to test for crude or partially purified extracts? If yes, what is rationale for it? Are there any references available which justify the testing of crude or partially purified extracts? 
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I agree with Nisha.  It depends on your research questions/objectives.  What are your hypotheses that should be tested, particularly in your research?
If you test all of them, you may get relevant information about antagonstic, additive, or synergistic effect of the different plant secondary metabolites compared with the activity of the purified compound. As suggested by Nisha, you can check using in vitro methods prior to in vivo study in animal models.
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I would like to estimate the serotonin level in blood plasma of fish. I am not getting any appropriate methods to do that. So can anyone help me out here?
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It is possible.  If you look at some older (1980-90's) publications, you will find HPLC techniques that utilized a fluoresence detector for the measurement of serotonin in nerves, gonads, and serum or plasma, but I agree with Professor Kong Li, the best detector would be electrochemical.
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Is the cells repairable after the damage? What is sublethal doses for cell lines, tissues, organs and animals?
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What are the differences between the structures of human hemoglobin and bovine hemoglobin?
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I hope you can find answer in these papers
Conference on Hemoglobin, 2-3 May 1957
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Brown fat produces heat metabolically in several mammals, but it is absent in birds. Recently some lizards have been reported to produce heat metabolically. Is it by brown fat?
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what are the parameters need to be measured for immunotoxicology study on broiler microbiota
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V D. Immunotoxicity Studies - FDA
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After exposure, we will extract blood and determine its ALT and AST levels.
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No feeding during the experiment will surely affect your results. To feed fish daily is as important as you also enjoy food everyday!
You can add this herbicide in fish feed formulation and just compare your results with control and treated. 7 day trial is too short for the true results, It should be of 90 days at least. 
Good Luck!
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Known and famous methods may be ancient:
1- Digestive Testing (Digestion Boxes) in vivo
2- comparison of the results of their nitrogen content, the beginning and end of the experiment.
There are new ways I do not know ..! Does anyone tell us about them?
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Dear colleagues, I have question related with regulation of lipolysis process in white adipose tissue;
do you know any isoform of adenylyl cyclase take part during lipolysis process in adipocytes of white adipose tissue  (particulary in the rattus) ?
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I ask about what kind of adenylyl cyclase isoforms taking part in cAMP production after adrenergic stimulation or other agonist of lipolytic transduction cascade, but Your answers includes information about enzymes involved in direct step of TG breakdown...
Does anybody could explain or indicate helpful scientific article?
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40º is the temperature of the oviduct in the hen, where the eggshell is synthesized, but i don't know if there's a biomineral that in physiological, natural conditions is made in a temperature greater than 40º...
Thanks in advance!
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Biomimetic mineralization J.Master.Chem.,2007,17,415-449 can help you dear
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I am working Western Blot on rat cells.
Thanks
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We use anti-Clock from DSHB http://dshb.biology.uiowa.edu/
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Hi, I measured homocysteine levels in  rat liver tissue homogenate with ELISA kit but I coldn't get results I think because of the homogenate's dansity, so I should dilute it. Is there anybody who have experience about measuring homocysteine levels in rat liver tissue with ELISA?
By the way, I am using CSB- E13376R CUSABİO Rat Homocysteine Elisa Kit (96 test). THANK YOU.
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Firstly, thank you for kind answer. According to this protocol, there is no need to extra  dilution tissue homogenate; but there is something missing. I have talked them; they accept that tissue need extra dilution which is not writing in protocol. That is what I wanted to ask. 
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When expressed in these two ways depending if it is heme content or pigment, heme iron is expressed in g hematine/ 100g muscle, g myoglobin/ 100g meat, g heme iron/ 100 g muscle (are this different?)
I would like to express my results in g of heme iron/ 100 g meat. Which would be the formula to use the factor above?
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If you consider that each myoglobin has only one iron atom inside it, and calculate how much myoglobin do you have in 100 grams of muscle. Similarly, if you calculate how much ferritin/hemosiderin do you have in 100 grams of muscle, maybe you can discover what you want, using the results in the factor that you describe in your question.
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Can someone please tell me reliable and simple methods to estimate minute quantities of glycogen, lipids and phophorus in an animal tissue?
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 Thanx a lot.
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Considering a basal diet, which are the nutritional requirements (% protein, fat carbohydrate and fiber) for zebrafish. 
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Dear Erick,
please find attached a number of reviews which represent all you need to know about zebrafish (as teleost paradigm) nutrition. The latest (Verri et al., 2016) is particularly useful to understand the fundamental impact and interplay of short peptides (oligopeptides) on nutritional pathways.
I hope you would please to receive this kind of input.
Moreover, never forget other "more practical" lab issues for zebrafish nutritional requirements, e.g. administration of "fresh" sources in addition to pre-made diets.
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Is there a universal method to measure the cholesterol content of biliary and fecal samples in mammals? I'm looking for a method to estimate total cholesterol content and that doesn't require a HPLC machine.
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Hi!
You could extract the lipids (by using the Folch or Bligh and Dyer methods, google will find these easily) and then use thin layer chromatography to separate free cholesterol as well as cholesterol esters from other lipids. These methods will require solvents (MeOH, chloroform, probably ether for the TLC running liquid), a stream of nitrogen (for evaporation of lipids without oxidizing them) and a thin layer chromatography running chamber, but not HPLC machine. These methods will probably give you more reliable results than any available kits, but do require some time to set up and may not be the best option if you only want rough estimates of cholesterol levels.
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Could saliva be used rather than serum to measure passive transfer of IgG1? Often a veterinarian is needed to take a blood sample which is why a noninvasive method (saliva) to measure passive transfer of IgG1 would be of use for the farmer to keep track of calf colostrum management. Thanks!
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Dear Dhia, Thanks for Your answer. Have you tried to correlate IgG Levels of saliva to those of serum of newborn calves? What is Your experience With using RID to quantify saliva IgG? Thank you for sharing knowledge:)
Julie
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I need some articles that can help me understand electromagnetism in different animals.
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You'll need to be a bit more specific about what you are asking. All living things generate electromagnetic fields. More complex organisms like mammals can generate numerous fields from various tissues. The gut for instance, produces a range of low frequency fields as muscular peristalsis moves food through. Other species have specialized organs that can generate/detect electric fields that can be used for sensing (lots of fish). Some can even generate such large fields that they can use an electric discharge as a weapon (electric eel). Some folks in my lab have measured various magnetic fields in animals using SQuID magnetometers. We also look at action potential propagation through tissues using the fluorescence of voltage sensitive dyes. There are most likely thousands of papers that discuss some aspect of electromagnetism in animals so it would be best to narrow it down a bit.
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In most chemical analysis for determination of a given compounds, protocol is usually, recommended a given pH if we do not confined to this pH we will not accomplished the desired reaction precisely at least..... are there interpretations   
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pH is obviously related to the presence of H+ ions which are involved in many biological and a biological reactions. Also remember the pH scale is logarithmic so each pH change of a unit representa a 10-fold change in H+ concentration.
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Humans as many animals are trichromats, so we can discern milions of colours from the visual spectrum. 
Some butterflies, but also many marine animals such as some mollusks and some crabs have many more, up to 11 (butterfly) or even 18 (mollusc). Why should these animals need so many if four are enough? There's a lot of puzzling on visual conferences and surprizingly, I have never heard the most obvious suggestion: spectrophotometry! Having many photopigments, one can potentially discern a mixture of colours (say yellow and blue) from a monochromatic one (green), which we can't. By this vision could aid smell even more than it does for us being much more discriminative in a chemical sense. 
Who would like to test this!!!
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Jacques, I believe butterflies perceive ultra violet radiation quite clearly, since the wing patterns of Colias butterflies differ considerably under ultraviolet light from their patterns discernible to our eyes. This is one way of separating otherwise identical species. 
Marc, to my mind, this is a very good line of questioning. The best way to understand this might be to first understand exactly how butterflies (and molluscs) interpret light related data- do they perceive it visually, as we do, or in some other manner? Next, how do they use this data? I remember reading something about an Australian swallowtail butterfly where females identify their larval host plant on the basis of the shade of green of its leaves. This is the primary identification mechanism. When the female approaches the plant, other senses decide whether it is indeed the larval host plant or not.
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I want to use of 120uM Torlox  ( water soluble analogue of vitamin E) and I want to know can I make solution and store it for two month?
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Well, in my opinion I wouldn't make the solution and store it for so long. According to our experience in laboratory, if you want to use it to obtain a calibration line, for example, I recommend that you make your solution almost immediately, not waiting for more than a week. 
Greetings!
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Can anyone explain the regulation of Leptin, Orexin and NPY for metabolism and growth out in teleost?
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@Mr. Asturiano: thank you very much..
@Mr. Kelany: it is interesting
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As we are interested to prepare the probiotic fermented milk, need to specify the milk we are using for the preparation. But, we don't have the clear idea about the milk we are using from the supplier. Can any one suggest me the confirmation test to differentiate the above mentioned milk types. Thanks for your concerned in advance... 
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Dear Vamshi... for the preparation of any milk product one has to do the standardization of milk for Fat and Solids-not-fat  (SNF) content and the same needs to be declared on the label ( This product is prepared from Toned milk or skim milk and so on.,) so that the product composition and other  properties would be maintained  uniformly, so the effect of composition of milk on product quality is nullified.
Coming to your question:
1. By organoleptic (sensory evaluation) one can make out the type of milk by its color.  Cow milk is yellowish creamy white in color, while  Buffalo and Goat milk  are of  creamy white in color ( Because: beta- carotene pigment  gets converted to colorless Vitamin- A, this conversion efficiency is less in cow). This color difference is  not an ideal test to differentiate in many cases (diluted or processed milk).
2. Milks of the closely related species can be differentiated by the precipitin test using antisera to blood serum proteins. with this one can make out  the "Fresh or  reconstituted milk  Reference: F. C. Pinto (1966). Serological differentiation of cow's, buffalo's, goat's and sheep's milks. Journal of Dairy Research, 33, pp 129-137. doi:10.1017/S0022029900011808. 
3. Hansa test helps to detection of adulteration of cow milk with buffalo milk ( by ICAR-National Dairy Research Institute)
4. ICAR-National Bureau of Animal Genetic Resources has developed a PCR based  test; this test is able to differentiate genomic DNA of cow and buffalo origin utilizing size differentiation of PCR amplified products from single set of primers simply by agarose gel electrophoresis.
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for example 2.826 µg /g (ppm) wet weight of Pb in liver = ???? µg /g (ppm) dry weight of Pb in liver
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Thanks for answer Svetlana,
But how can we build a calibration curve? I have lot of data ie, different concentration of heavy metals in different tissues, how can i change them? Can you explain again with examples? 
Thank you so much 
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I want to measuring motor evoked potentials (MEP) in rats using TMS and surface EMG. Typically in humans 50 microvolt (peak-to-peak amplitude) is a good indication of a positive MEP. However, is it reasonable to also assume this for rats? What I could find from the literature is that 15-20 microvolt was used as a positive MEP for measurements recorded from the front limbs. Would this also suffice for hind limb measurements?
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Julia, MEPs are elicited electrically or with TMS in the motor cortex of humans and primates. Rats, mice, other rodents, cats, and even certain monkeys do not have a monosynaptc corticospinal tract onto the spinal motorneurons. Therefore, even if you may elicit some potentials by stimulation of the motor cortex (M1 for instance) the meaning may be completely different. I know that people say that they elicit MEP in rodents, the elicit something indeed. I'm not sure what it is, and I know that has a different meaning than human TMS. I tried transcutaneous stimulation of the cortex about M1 and got some potential in the gastronemius, but the potentials were much more powerful when I stimulated the brainstem. It is known that all these animals have various tracts that establish monosynaptic inputs with spinal motorneurons. In summary, I do not think that human and rodents are comparable in this respect. 
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For functional analysis of certain miRNAs in bovine follicular development/ ovulation, I want to perform in vivo experiment by delivering the LNA microRNA or LNA inhibitor into the cow. I need technical advice of feasibility and modus operandi of this experiment in bovine; for instance way of delivery, point of delivery LNA microRNA or LNA inhibitor …
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Thank you Jack Haiden Britt for input.
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Mu-crystallin (CRYM 16p13.11-p12.3.  in human)  is a lens structural protein in diurnal marsupials and an enzyme in mammalian possible involved in the potassium-ion recycling system; in addition it is a mammalian homologue of Agrobacterium ornithine cyclodeaminase..
In mammalian forebrain ketimine reductase was identified as mu-crystallin. It was also seen that CRYM encoded "adenine dinucleotide-nicodinamide phosphate (NADPH) -regulated thyroid hormone-binding protein (THBP)"; this identifies a new role for thyroid hormones in regulating mammalian amino acid metabolism.
There are many publications that correlate these enzyme activities to  various pathological events.
Analysis of human tissues detected abundant expression of CRYM in heart, brain, skeletal muscle, and kidney, lower expression in lung and liver.
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Using radioisotopically labeled P5C, we  showed that proline inhibitsf P5C reductase activity.  However, we never studied P2C reductase.activity.
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Hormones: estradiol, progesterone, testosterone and cortisol. Thank you very much.
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Hi,
I agree with Allison, Cayman Chemical is a good choice!
best regards,
Hanna
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I'm working on my thesis and I would like to find the prevalence of subclinical ketosis in dairy cattle by measuring acetoacetate in urine. However, I have not found any information about what the normal levels of this ketone are. Thank you.
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Dear Mateo,
If you want to find the prevalence of subclinical ketosis in dairy cattle, there is a interesting and cheap device that already has been evaluated for that proposes (IWERSEN M., FALKENBERG U., VOIGTSBERGER R., FORDERUNG D., HEUWIESER W. 2009. Evaluation of an electronic cowside test to detect subclinical ketosis in dairy cows. J. Dairy Sci. 92: 2618-2624.), It is a cowside test that measures B-hydroxybutyric acid concentrations (quantitatively) in whole blood and gives you the information in 10 seconds, we have had excelent results using that ketone-meter (Precision Xtra, Optium Xceed or FreeStyle Optium are the names of the device according to the Abbott selling area), I strongly recommend you to read that paper before you start measuring ketone bodies.
Best wishes
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I am looking for non-destructive method for analyzing pesticide contamination in birds of prey, can we use fecal sample and pellets for analyzing pesticide contamination? 
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another non invasive biomonitoring tool are feathers... maybe this publication could be useful.
best regards
stefania
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We are analyzing fish bile acids by LCMS and are interested to quantify each bile acid. What internal standard is most suitable. What are the marker ions for conjugated and unconjugated bile acids? 
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Jaundice is a common clinical disorder in tropical countries like India. It is defined as yellowish discolouration of skin, sclera and mucus membrane due to increase in serum bilirubin concentration which affects the liver function.  For this purpose liver function parameters are estimated in 100 subjects suffering from jaundice to evaluate the clinical utility of these tests to differentiate hepatocellular jaundice from obstructive jaundice.  Serum total bilirubin with its fractions(both conjugated and unconjugated bilirubin), ALT, AST,ALP, GGT and albumin are  analysed by standared methods. Statistical analysis can be done by student ‘t’ test(unpaired-t test) and ‘p’ value is elicited. Results :. Conjugated bilirubin, ALP & GGT are  much more significantly increased in obstructive jaundice(p<0.001). Unconjugated bilirubin, ALT & AST are significantly increased and albumin levels are significantly decreased in hepatocellular jaundice(p<0.001). 
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Hi, I'm running Western blots, looking at various proteins involved in the mTOR pathway and I'm looking at phosphorylated versus total protein ratio.
I have 8 replications (animals) and 4 treatments and am using gels with 15 wells so I can only load 3 reps (each with their 4 treatments) per gel.  I'm using the same procedures but sometimes exposure times will differ somewhat on each occasion.  
What would be a good way to normalize between different gels? How can I account for differences between gels. 
I was also wondering if anyone ever uses a positive control and normalizes to that.  Right now my data is organized as phosphorylated protein as a ratio of the positive control (which is a pooled random muscle sample), total expressed as a ratio of the positive control  and then the final value is a ratio of those ratios as in Phosphorylated versus Total.  
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You could include an internal standard in the samples that are run on the gel and compare all band intensities to the intensity of the standard. An approach I have taken is to add some purified immunoglobulin from the same species as my primary antibodies into every sample at the same quantity. The secondary antibody detects the IgG, giving a comparator, requiring no additional wells, and also controlling for differences in sample loading.
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I am in need of normal reference values (like we have for humans,) for various biochemical parameters in adult male albino wistar rats, like serum glucose,plasma insulin, HbA1C, SGOT, SGPT, ALP,UREA, CREATININE, ALBUMIN,  LDL, HDL,TOTAL CHOLESTEROL,TRIGLYCERIDES, VLDL and in vivo liver antioxidant enzymes like SOD,CAT,GPX ,LPO. Please provide me the values with proper references. thanks.
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In case you use Charles River as your supplier, they have published those data also, even separated for their different breeding facilities. In case simply contact your local CR representative. If you do not use Harlan or Charles River animals, I would suggest to collect as many data as possible from the different breeders and have a look on the variability of the parameters.
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How does silicon help the human body?
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It's a good question, Pankaj. I know Si plays important biological roles in plants such as resitance against diseases and pests.
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I am looking for articles dealing with dragonflies dyes or dyes in other order of insects.
Any suggestions? Thank you.
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Red cotton bug and dusky cotton bug (Hemiptera)  always stain the cotton fiber. They have importance from the view point of dye. Cochineal scale is well known for insect dye for food and drinks.
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We've performed thermal coagulation of bulk (~4x4x4 cm) porcine muscle, LD (loin) tissues using two different heating protocols. In the first one, the sample was submerged into a jar with boiling water and heated for ~ 40 min, until the internal temperature reached 85-90 deg C. In the second one, the sample was inserted into a Ziploc bag and then into the jar with boiling water following the same heating time with the same end temperature. We've noticed that these two protocols triggered different changes in optical scattering of the samples. BTW, water loss was the same in both cases.
I'm wondering what kind of changes in the sample structure, morphology, biochemistry etc. do these protocols introduce such that they are manifested in optical scattering. Or, perhaps just tell me what is (or can be) different in these samples, and I'll try to relate it to optical properties by myself:) Also, any resources analyzing different methods for thermal processing of meat will be helpful.
Thanks in advance!   
P.S. Details of optical measurements and the method for extracting optical absorption and scattering of tissues can be found here:
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Thanks for sharing your question with me, but can only make a guess and add some of my brainstorming thoughts:
1) direct contact of raw meat with water may have some osmotic effects, which otherwise where prevented by the plastic bag. Even without boiling, muscle fibres and cells may have some changes in first osmotically attracting water (for example, like red blood cells explode within 30s of distilled water, at room temperature), but just diffusing water may also have some effects, rinsing mobile ions out of the tissue. This direct contact effect with water may be responsible for some changes on the surface, but perhaps in the deeper tissue of your sample - but at the end, after reaching the temperature of around 90 degrees, the
2) assuming that you used some vacuum pump to remove any isolating air bubbles, the plastic itself may have a different temperature transporting capacity (there might be a better expression..) I mean, the plastic can isolate, therefore leading to a different time curve of how fast the denaturation process goes through the meat... (what happes if you use 2, 2, 3, 4 ,5 plastic bags at once - any delay of temperature increase? The final temperature should be met, but at a slightly later time point (?).
3) I could be wrong and anything else is more relevant.
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In large animals like cattle, sheep, etc. 0.1 ml of 1mg/ml Johnin PPD is generally used, but for mice, which concentration and dose will be suitable for DTH test?
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I think it should be 1/10 of the dose of large animals as in case of brucellin we use 1/10 of the dose of large animals to guinea pigs
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I provide mix buffer containing 100 mM glycine, 100 mM tris, 100mM succinic acid and 100 mM imidazole with ph 3, 3.5.....9
25 microlitr enzyme in tris buffer with ph 7.5 was mixed with 50 microlitr mix buffer and incubated in 4 C for 2 h. Then I add 75 microlitr substrate and assay thier activity in specific time and tempreture.
I think I went wrong way.for determining ph stability, all of my samples should reach the same ph (ph optimium) finally and after that I could assay thier activity, shouldn't they?
How do samples with different ph reach the same ph finally?
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At first, the optimal pH and temperature of enzyme activity must be determined. For pH stability, enzyme solution was pre-incubated at different pH in the range of 3.5–9.0 for 30 min at optimum temperature for enzyme. The residual enzyme activity was determined.
Read the attached papers
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Kindly suggest me a simple protocol to count protozoa from rumen fluid.
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Hi
This is the protocol used in my lab. It is long (15 minutes per sample) but it is very reliable.
Good luck
Ruminal content (approximately 1 L) was strained through 4 layers of cheesecloth and a 5-mL portion of the strained ruminal fluid was preserved using 5 mL of methyl green formalin-saline solution for protozoa enumeration (Ogimoto and Imai, 1981). Protozoa samples were stored at room temperature in darkness until counting. Protozoa were microscopically enumerated using a counting chamber (Neubauer Improved Bright-Line counting cell, 0.1 mm depth; Hausser Scientific, Horshamm, PA) and genera were identified as outlined by Dehority (1993).
References
Dehority, B. A. 1993. Laboratory manual for classification and morphology of rumen ciliate protozoa. CRC Press Inc. . Boca Raton, FL.
Dehority, B. A. 1993. Laboratory manual for classification and morphology of rumen ciliate protozoa. CRC Press Inc. Boca Raton, FL.
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Multi-cellular organisms have obvious advantages & larger cells would have severe limitations. But NEVER in any place & time there could be a species where individuals are huge cells! Why? Volume - surface ratio is one of the answers I have seen in some of the text books. Not convinced completely though. A few websites/scientists have some answer; I have some thoughts. But wonder what are your thoughts on this!
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Kshitish, in order to answer your question we would have to look specifically at every cellular mechanism and try to examine its design at larger dimensions. In some cases it might do well but not in othes. Take for example a cell the size of a mouse. Do you think the same 100-nm lipid bilayer membrane would be able to hold a 20-gram protoplasmic soup? Possibly not, and soon you’ll realize that in order to get a cell that size you’d have to change the typical eukaryotic cell design, possibly creating some kind of powerful exoskeleton for the cell to be able to hold the 20-gram soup without spilling. So let’s say that such a cell might look like a huge walled plant cell. Now, let’s say that the cell needs to respond to an extracellular stimulus, say food source, predators, or physical threats like heat or cold. A typical cell that uses cAMP, calcium currents, lipid messengers like IP3 or Na+ or K+ signaling might respond in milliseconds but for the baseball ball size cell, it might take 10 seconds to convey the signal through 2 inches of the aforementioned 20-gram thick soup. Now you have a cell that not only can easily break apart but also is slow to react. It might still work though but when you start to add up features, you need to grant further concessions and you end up with some really weird stuff. You might model it using computer models and it might still work in isolation but the only way to prove whether the design has relevance in the wild, is to do a field test. I’d suggest starting with computer models and if the design holds then testing it in the wild is the next step. By the way, all of this falls within a new discipline called Synthetic Biology. Good luck.
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In my opinion, on the contrary, they activate because the goal to a perceived action was attributed (understood) previously. If the goal is attributed, then MNs activate. If the goal is not attributed, they do not activate. If MNs processed the goal they would activate regardless of the presence or absence of a goal. To be responsible for a phenomenon a neural structure should activate during this phenomenon. What do you think about it?
You can look through my article:
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Thank you; Katalin; for your interest. I just supposed that when we are shocked by a bear, we do not reflect her actions in our MNs, but trigger a flight-or-fight reaction. It has not been studied yet.
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Prions are dangerous misfolded infectious proteins - which I read in an article about mad cow disease. Up until prions I used to think, only nucleic acids could be replicated into this earth. How can prions can do so without DNA? I can not accept it. You know they are crazy like zombies... I feel like investigating more on this topic to find out in which way they are multiplying themselves and becoming harmful. If you know about their mechanism of virulence please share with me..
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It is not that the prion protein replicates itself. We all have the native form of the prion protein in our brain. problems actually start when some of the prion proteins get misfolded into a form that aggregates (the infectious form), which also induces misfolding in the native protein, increasing the amount of aggregates, and inducing more and more of the native form to misfold.
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see above
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Mattias:
I hope this question gets a lot of interdisciplinary responses because I believe it touches on a number of interesting, if not sometimes paradoxical, conditions.
For example, it has long been held that there is an apparent inequity within the order Primates in their need for UVB light and resultant synthesis of vitamin D3. New World primates are generally far more sunlight-dependent than their Old World counterparts, and the frequency of observable metabolic deficits in UV-deprived New World primates would seem to validate this. Therefore, is there a greater ability for Old World monkeys to satisfy their metabolic calcium requirements solely through diet? If so, what is the nutritional source? What evolutionary processes bought about such a discrepancy between Old World and New World primates?
Secondly, the degree to which nocturnal animals may be absorbing UV light while at rest (during the day) should not be overlooked. While touring in Costa Rica I was very surprised to see sloths sleeping high in the trees fully exposed to sunlight. While very nocturnal in behavior, this taxa certainly seemed to have ample opportunity to absorb UV light. I’d postulate that other species do likewise.
Lastly, on occasions of having to hand-rear infant armadillos, it has been found that those infants being reared in the absence of UV light tend to fair very poorly and show evidence of metabolic bone disease (as one would expect from a calcium deficiency). Others raised on the same diet and exposed to sunlight on a regular basis have faired much better. The paradox lies in the apparent requirement for UV light exposure by infants of a nocturnal, subterranean taxa. Is vitamin D normally passed from mother to her nursing infant through the milk and, if so, how is the mother armadillo synthesizing vitamin D?
My apologies for raising more questions while providing no answers. The question opens a number of intriguing side topics.
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I generally use paint but it's not enough for advanced biological structures.
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Easy free-ware for a 3D look is Sketch-up. I start my drawings there. Only spheres are complicated, so after having drawn separate objects I merge them in Photoshop and add spheres when required.
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The old concept says there might be 3 or 2 but new concepts say there will be only around 2.5 or 1.5.
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According to my knowledge, the modern textbook meaning is that 10 H+ are pumped per molecule oxidized NADH. Moreover, it is general believed that 4 H+ are demanded for the synthesis of 1 ATP. Consequently, 2.5 ATP per NADH are formed.
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I want to deliver antiviral plasmid into shrimp via feed. Is that possible to integrate the plasmid into animal feed without degrade all of plasmid. What methods that I must use?
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Dear Danang,
the important point is to use a vehicle that will highly ciompact and protect the plasmid DNA.
I'm thinking of two options:
the first one is to use a liipd-based that highly compact nucleic acid (such as DreamFect Gold)
the other one is to use magnetic nanoparticles: this was demonstrated some times ago by delivering DNA into jejunum with PolyMag beads (Plank C., Expert Opin Biol Ther. 2003) and also by protecting AdenoVirus into stomach using ViroMag Beads (Scherer F., Gene Ther. 2002; 9(2):102-9).
The important point of the later method is that organims can be immobilized onto a magnetic field in order to enahnce transfection.
If you need any data or information do not hesitate to contact me:
good luck with your experiments,
best regards,
Cedric
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I am trying to establish cardiac cell or cardiomyocytes isolation and culture from a mouse heart. I need a convenient protocol, if somebody can help me out. As far as I know the heart has to be isolated fresh and proceeded. Can we try storing heart tissue at -80?
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Hi, I'm a little bit late..... I'm working on isolated adult mouse cardiomyocytes. I transduce a FRET sensor, therefore I need to keep them alive for at least 3d. See my protocol attached
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In an experiment adding inhibitors sample with cyanide added sperm cells were more motile and motile for longer than controls.
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Insect sperm are a little different, they do not have mitochondria. Some do require oxygen but many species rely on glycolosis for ATP production
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I am looking for the routine biochemistry analyzer for liver function tests. I need it for rats therefore it should require small amount of blood. Also I want to measure prothrombin time. Please suggest a good and cheap device on the market with light exploitation features. Thanks.
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yes you can use autoanalyzer for liver function tests. For example, ROche, Siemens, Abbott, Beckmann and Olympus are auto analyzer and thera are commercial kit for tests.
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Can anyone suggest a method to protect a peptide from being hydrolized by digestive enzymes in the digestive tract of penaeid shrimp, keeping its functional activity as modulator of glucose metabolism?
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I suggest you to encapsulate the peptides of your interest with appropriate nanoparticles or nanomaterials.
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Are you refering to plasma/serum or tissue samples? In the right preservative at -20 degrees, most proteins including SOD and CAT will be preserved for about a month in tissues or even longer at -80 degrees. I store my tissue samples in RCL2 at - 80 degrees and have measured proteins and mRNA levels after almost 3 months.
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Guide me.
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If you are not using a blaberoid cockroach the clotting issue is almost non-existant. Species of the Blattidae and Blatellidae can be bled without or with minimal dilution using a capillary tube to collect the drops of serum coming from a coxa that had its femur autotomised by gentle tugging. The serum can be collected by centrifuging the serum in micro-centrifuge tubes and a small crystal or aliquot of PTU solution added to prevent melanization.
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I'm unable to get the yellow colour for GSH estimation (by ellaman's et al). I'm standardizing through rat's liver and rat's kidney. I'm preparing 10% homogenate, centrifuging it and using the supernatant I'm carrying out the assay. Once I add ellaman's reagent I'm unabe to get that straw yellow colour. However my glutathione standards are giving out excellent results.
Where could I be going wrong?
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As there is no problem with reagent, there might be a problem with the homogenate preparation or buffer in which the homogenate is prepared.
May be there is some coloration, but that might not be visible because of homogenate color.
So, please check any reference paper and which percentage of homogenate (may be lesser) is required for these type of colorimetric assays.
Good Luck..!!
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I have to sacrifice pretreated mice models to evaluate the mechanism study. Before killing them I have to collect blood for GTT. I've been informed that I have to give them an interval before killing them (I do not want to make them stressed). Also I need time to collect blood from all of the mice models.
1. I need to know that how long the interval should be before killing them?
2. Should I collect blood from all mice of same group in same day or should I collect a certain number of mice from all of groups?
3. Should the killing order be maintained the same as the blood collection or is random order fine if the interval is about 3-4 days?
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I really don't know much about your experiment from the information you've provided however my suggestion would be:
1) Use the interval period used in previous literature, assuming that the method has been done before
2) Depending on your time constraints and how many animals you have, will determine how you collect. I'm assuming you have a lot of animals, so perhaps it is better to take a sample from each group on the same day rather than taking one group at a time. This should help you control for changes across days between groups and perhaps see if there are any changes across time within groups.
3) Not really sure about this one. Again I would refer to previous literature. I would think that after the interval where animals have returned to baseline stress levels, it shouldn't matter which order you kill them.
I Hope this helps you
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There are a lot of papers about GnRHR expressed in several tissues, including prostate, ovary and mammary cancer. But it has been difficult for me to find a reference about its localization (protein or mRNA) in testicular tissue.
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Hi Gloria,
If you have not see already, here are some references that may like!
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I would like to estimate total protein from crab muscle tissue samples and would like to know if a chilled centrifuge is necessary (my lab does not have one). I plan to use the Pierce* 660 nm Protein Assay in order to quantify the amount of protein.
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I suggest the following: It may be that crab muscle has a lot of connective tissue. After you homogenize (BTW, are you using a Dounce-type homogenizer or a motorized bladed shredder-type?), pass the homogenate through several layers of wetted gauze. That will remove a lot of the gunk. 20 min @ 15K spin is standard for pelleting crude mitochondria. You don't need that. 600 to 1000 X g for 10 min is sufficient for a crude homogenate for total protein assay.
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A number of studies have suggested that pharmacological compounds such as resveratrol, which activate (among others) SIRT1, can improve longevity in rodents and also metabolic function in obese rodents and humans. However, recent data (see attached) suggests that the over-expression of SIRT1 does not improve skeletal muscle insulin sensitivity, does not have an additive effect to caloric restriction and has no significant effect whole body metabolism. Additionally a number of reports have questioned the specificity of resveratrol as a SIRT1 activator which leads to the question of how relevant is SIRT1 in the physiological regulation of insulin responses and metabolic function?
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David:
Thanks for this intriguing question.
I would note however that this data (the UCSD study from White et al. [1]) is not compelling given some methodological concerns that emerged upon my critical appraisal. Essentially what was tested was an insulin-normal model in lean young mice, but this does not in any way exclude a positive effect from muscle SIRT1 overexpression in what I would consider a far more clinically relevant insulin-resistant model; indeed, the clinical relevance and applicability - should these results ever be confirmed with true human clinical data and not just in preclinical animal studies - of absence of muscle SIRT1 overexpression is wholly unclear when observed in the absent of any significant insulin resistance. And even more critically, the UCSD White et al. results stand against several lines of contradicting evidence, as for instance the conclusion drawn in the Chinese Academy of Sciences study [2] that increased expression of SIRT1 did in fact improved insulin sensitivity, especially under insulin-resistant conditions, and with resveratrol apparently acting as a SIRT1 activator, enhancing insulin sensitivity both in vitro in a SIRT1-dependent manner and also preventing high-fat-diet-induced insulin resistance in vivo.
Furthermore, germline overexpression of SIRT1 was observed in the UCSD study (acknowledged by the investigators), in addition to large-scale (~150-fold) SIRT1 overexpression, leaving open the possibility that beneficial insulin modulation may be preempted under such specialized conditions of chronic SIRT1 overexpression and/or aberrantly large SIRT1 overexpression. White and co-authors try to counter this, implausibly, by noting that a previous Columbia University study [3] found that muscle insulin action was unaffected by two- to threefold SIRT1 overexpression from germline, but that is clearly a vastly smaller magnitude of SIRT1 overexpression (2X - 3X) from that observed in the UCSD White study, running at ~150X-fold, and no extrapolation therefore can be legitimate here.
In closing let me add that it's beyond the scope of this brief response (the last time I reviewed these issue late last year, the review ran to 85+ pages with 28 pages of references (300+) to enter authoritatively into (1) the association of SIRT1 with caloric restriction, (2) with whole-body metabolic status, and (3) whether resveratrol exerts true SIRT1 molecular activation, but I am not based on the preponderance of evidence convinced that these associations have been plausibly challenged by methodologically robust data (multiple reviews I critically appraised conclude the opposite), nor that SIRT1 activation is not observable in resveratrol operation (especially when we differentiated dose-dependent effects as per the recent Harvard/NIH study [4], among others). But that's another story. In the here and now, under critical review the UCSD study results do not materially affect the balance of evidence given unresolved methodological concerns, and the presence of a non-trivial body of contradicting data.
1. White AT, McCurdy CE, … Schenk S. Skeletal muscle-specific overexpression of SIRT1 does not enhance whole-body energy expenditure or insulin sensitivity in young mice. Diabetologia 2013 Apr 19.
2. Sun C, Zhang F, Ge X, et al. SIRT1 improves insulin sensitivity under insulin-resistant conditions by repressing PTP1B. Cell Metab 2007; 6(4):307-19.
3. Banks AS, Kon N, Knight C, et al. SirT1 gain of function increases energy efficiency and prevents diabetes in mice. Cell Metab 2008; 8(4):333-41.
4. Price NL, Gomes AP, Ling AJ, et al. SIRT1 is required for AMPK activation and the beneficial effects of resveratrol on mitochondrial function. Cell Metab 2012 May 2; 15(5):675-90.
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Researchers identified the human immunodeficiency virus (HIV) as the cause of acquired immune deficiency syndrome (AIDS) two decades ago. Since then, the search for an effective vaccine to the deadly infection has received more funding than any other vaccine effort in history. And the search, employing ever more innovative strategies, continues. Skeptics say no vaccine will ever be found.
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The focus is now on working on latent virii. To target the virus hiding in reservoirs like gamma delta CD-4 cells in the GI tract. The problem is to find a suitable drug which can target these sites and other similar sites or to flush the virus out these revoirs when the active drugs can work. Lot of dat have been prented recently in Atalanta CROI meeting.
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Pepsin -
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Dear Vicki, Thank you very much
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I would like to compare my results with reference values.
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Dear Faiz-ul: Thanks for your answer. I need to know biochemecal profiles in laying hens on blood (AST, ALT, Total protein, Albumin, H/L ratio, etc). I need to compare the values founded in my work with reference values. I only found these values on broilers but not in laying hens. If you know someone who works on this topics please if you tell me I`d appreciate. Best regards