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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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can Anyone explain about this method?
thank you 😊
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RNA pull down assay is a popular RNA-centric approach to study RNA-protein interaction.
This assay depends on the principle that streptavidin agarose bead has a strong affinity to biotin-labeled RNA and can effectively and specifically pull down biotinylated RNA–protein complexes. The proteins eluted can then be detected by western blotting or mass spectrometry.
RNA pull-down assay selectively extracts a protein–RNA complex from a sample. Typically, this assay takes advantage of high affinity tags, such as biotin. RNA probes can be biotinylated, complexed with a protein from a cell lysate, and then purified using streptavidin agarose or magnetic beads.
Alternatively, you may label the protein, or the RNA–protein complex may be isolated using an antibody against the protein of interest.
Best.
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What is the need and importance of doing morphological physiological and biochemical analysis?
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This question cannot be answered, it is very broad and unspecific. You might as well ask "What is the use of analysis" or "What is the use of science"'
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If not, we are going to standardize A25 autoanalyzer, kindly suggest kits for measuring biochemical parameters like liver function parameters (Bilirubin, total protein  AST, ALT, ALP), urea, creatinine....
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No,there are seperate kits to measure biochemical parameter
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Hello!
Ive been trying to use the ninhydrin assay to measure concentration of PEIMax accurately after dilution. PEIMax is deacetylated 22kDa linear PEI*HCl so it should only contain secondary amines and should supposedly only form yellow compounds that absorb at 440nm with ninhydrin reagent. When I run the ninhydrin assay with PEI however, i see an obvious purple color and i can make wonderfully reproducible and linear standard curves using either 440nm or 570nm absorbance. I am using the Sigma 2% ninhydrin + hydrindantin in pH5.2 LiAc, reacting at 80C for 10 min in a PCR plate sealed with nitrogen blanket (https://www.sigmaaldrich.com/US/en/product/sigma/n7285).
Anyone have any ideas as to why I might be seeing such strong absorbance at 570nm even though i dont have any primary amines in the sample to form Rheumann's purple?
Another point I suppose that might be worth mentioning is I reconstitute my PEImax in 0.1M HCl however Ive run HCl alone in the assay and not seen any color change.
Thanks in advance!
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We use R&D Proteome Profiler Rat Cytokine Array for detection of multiple cytokins in tissue samples. The standard protocol utilizes streptavidin-HRP with a chemiluminescent detection reagent that is not specified in the product documents. Does anyone know, what is the two reagents provided to the kit (chemi reagent 1, chemi reagent 2)?
Have anyone tried another detection system for visualizing (either chemiluminescent or other) the dots?
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We use R&D Proteome Profiler Human Cytokine Array for screening different cytokins. Chemi reagent 1 is hydrogen peroxide and Chemi Reagent 2 is a stabilized luminol.
For your question about using different detection reagents,
Yes, we used Thermo Scientific Pierce ECL and it works perfectly well.
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Profound biochemical analysis into the structure of a certain protein can explain and even predict the mechanistic properties of said protein function and even of many more proteins that have a similar fold. What other biological molecule type (not protein) is an example of that same logic?
I was thinking that maybe phospholipids' structure or phosphorylation state can say something about its function, does it sound right?
I would appreciate it if you have another example
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For small molecules, the chemical reactivity can be predicted by what functions groups are present, and how they are connected (covalent structure). This is not sufficient for proteins - they are composed of only 20 different amino acids, therefore they all contain the same functional groups - you have to know the 3dimensional arrangement of the peptide chain bringing the correct functional groups into a very specific arrangement to explain their activity, and unfolding (denaturation) of the protein leads to loss of function, although this does not alter the covalent structure. The next most similar system are ribozymes, where the sequence of nucleotides determines the folding of the chain, which in turn produces the exact 3D structure required for function. The most prominent ribozyme of course is the ribosome, where not only the tertiary, but also the quaternary structure is essential for proper function and regulation.
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Palmyrah fruit pulp has a bitter taste due to this saponin, so I have to remove the saponin with a cheaper method which can be applicable to the fruit industry.
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add naringinase enzyme
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So i need to compare the digital analysis intensity with the photometric absorbance of Cu bentonite samples. Do i just need the Blue value in imageJ? Do i have to use all 3 and compare with different plots?
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Hi Anastasios Mazarakis . Do you happen to have an image of your sample? This will help us better understand what you want to do. Thanks.
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The prevailing theory is that cancerous tumors reflect a form of cellular natural selection, where random mutations confer evolutionary advantages to tumor cells. These survival benefits accumulate over time, eventually empowering tumor cells to outcompete healthy cells and defeat the immune system.
Given this theory, one expects a correlation between cell division rate and cancer rate -- tissues with the highest number of cell divisions should show the highest incidence of cancer (environmental and hereditary factors notwithstanding).
However, few papers seem to verify this assumption, or even document cell division rates and lifetime cell divisions among different tissues.
These are the two best papers so far:
However, the same senior author leads both papers, and the papers seem to omit the most common cancer types, breast and prostrate. Furthermore, the methodology seems fragile as they conducted an analysis across different studies that may not have employed uniform methods.
Could anyone recommend more robust or authoritative papers on the subject of cell division rates?
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I wish you Mr Clarence Hu to be a doctor very soon . Best regards.
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Is a higher electrode area beneficial for electrochemical impedance spectroscopy (EIS)-experiments?
And should the electrodes be placed further away from each other or is it better if they are closer to each other? If so then why or why not?
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Dear Frederik-Lesniewski,
EIS-measurements[1,2] share, nearly, the same constrains as the quasi-DC-measurements, as well as the, more widely known, traditional, DC-measurements[3].
Specify, please, what are your own specific material's/device's (electrical resistivity) constrains related with (or constrained by) the EIS-measurements[4] e.g. due to either your EIS-setup (specs[4]), or even your cell's constrains ?
2. How to measure conductivity and which type of conductivity sensor to choose https://visaya.solutions/en/article/how-to-measure-conductivity
4. Two or four electrodes EIS-measurements ?
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I have a particular protein that I'm interested in which acts on cardiomyocytes. I'm interested to find out whether this protein activates the Toll-Like Receptor signalling and JAK/STAT signalling. What biochemical analysis would you recommend I carry out to find this out? What are the readouts that are commonly used? The signalling pathways field is completely new to me so I apologise for the naivety of this question.
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It is quite possible with flowcytometry. If you want to check signalling via these molecule you must treat your cells with the specific stimulant followed by fixation and permeablization and surface/intracellular staining. The sample can be acquired on flowcytometry and it will give you relative results (upregulation/downregulation in comparision with controls).
If you want to perform flowcytometric assays for these signalling, let me know. I will send you references.
All the best.
Jitendra
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I analyzed the internal standard "2-methyl-L-cysteine hydrochloride" using HPLC and the chromatogram shows three peaks instead of one which is weird!!
I repeated the preparation process two times to check if there is a contamination problem but the chromatogram still showing three peaks. So what do you suggest?! Is there a possibility that the internal standard is converting to other compounds?!
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Dear Rawaah Y. Al-sharrab,
Thank you so much for your interest. Actually, it is very difficult to solve the problem of internal standard. That is why, most of the researcher are now developing their method using external standard and to use matrix matched standard for avoiding the use of internal standard. Anyway, if you interested to work with internal standard, try to use the solvent as same as mobile phase, it may helps to minimize the problem. I read the answer made by
William Letter, he described many things, you may follow his advice. Thank you.
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How can/should we distinguish between a Biochemical and a Chemical Reaction.
As per one explanation:-
Chemical reactions are discrete reactions with catalyst involved in the process where as in biochemical reactions there are a series of reactions involved with the product of one acting as the substrate for another and this complex process of interchanges taking place with the involvement of enzymes.
For a more specific example if we are conducting photosynthesis in vitro then it will be considered as a biochemical reaction rather than a chemical reaction.
But the dilemma stems from the fact that, even chemical reactions go through complex series of steps, like any organic synthesis reaction. In this case also there is the involvement of catalysts like enzymes. Thus, can we consider it as a biochemical reaction! But mostly we only attribute it to be a chemical reaction which is indeed the case.
So, what is the proper difference or point of distinction between a biochemical and a chemical reaction. How can we exactly relate that one reaction is a biochemical and the other is chemical!
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Dear @Mrutyunjaya Panda All biochemical reactions are chemical reactions. I agree with Dr @Frank T. Edelmann in that in principle, there is no major difference. The same reaction can occur 'in vivo' and 'ex vivo'. You can also access a similar discussion at the following link:
Best wishes, AKC
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I would like to say delta Hº or delta Sº. What I cannot see if it is Hofmeister. Delta Hrº?
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I’m using ARPE-19 cells to test the levels of inflammatory cytokines (IL-6, TNF-alpha). My protocol:
1. Seending 16,000 cells (500 uL, per well) in 24 plate
2. Treat drug 12 h
3. Treat H2O2 200 uM 24 h (to induce the inflammatory)
4. Take the supernatant of the cells and use ELISA kit to test IL-6 & TMF-alpha
In the result, the absorbance of the control group (untreated one) was too low (much lower than the detection limit refer to the calibration curve).
I would like to know how to increase the level to get to the detection limit?
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Dear Yir,
I agree with Anton, that this is very valid data! If indeed you think that your cells should be producing some TNFa at a basal level, perhaps you could increase the cell density. We would use 10,000 cells in a 96 well plate (BV2-microglia). So, if your cells would be ok with it, then it would work. Note though, it will also increase the release from your stimulated group, so you might then need to dilute it keep it in the dynamic range of your assay. :-)
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Reduced GSH oxidizes rapidly, what should I do to aviod oxidization during the biochemical analysis of tissue sample? I found some method to measure it are based on Ellman reaction, however this reaction is for all available thiol group, how to explain it?
Thanks in advance
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Hi, Ellman sometimes used as a measure of total thiols as the regent DTNB reacts with a thiol group, bur, using TCA in the procedure or precipitating all other thiol protiens will make the measurement more accurate.
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Where can i learn rat dissection for brain tissue biochemical analysis, mainly the experiment room and surgical tools setup
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hi.you can found all of your needs in Paxinos Atlases
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I'm designing a low-grade chronic treatment with this cytokine and I'm wondering how regularly to change the culture medium based on the half-life of the protein in an in vitro environment.
Thank you in advance
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It almost certainly depends on each vendor's individual preparation. We have published one example using our own TNFa preparation:
If your vendor is not so forthcoming, it would be best to develop a bioassay and see for yourself.
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Am in Peptide / Protein Research, may i know what useful analytical information we are getting from 13C & 1H NMR spectroscopy analysis?
Somebody getting NMR for smaller proteins, any useful information we will get it from this?
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In general, NMR is very informative and powerful technique. You can estimate the relative amount of your peptide/protein, the purity of the sample, or even the fold of the peptide/protein. You can also do interaction studies or stability tets.. Recording simple 1H spectrum can already tell you such information. But there is much more NMR can do. I would recommend to start with this very nice book:
NMR of Biomolecules: Towards Mechanistic Systems Biology
Editor(s):
  • Prof. Dr. Ivano Bertini
  • Kathleen S. McGreevy
  • Prof. Giacomo Parigi
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How would I know exact pore size of agarose if i make X% of agarose? for example I made 4% agarose then what would be pore size of agarose gel?. Please give your valuable inputs. Thanking you!
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I am using strain AH109 to do Y2H. I contructed my protein into pGADT7 vector, and co-tansformed it with empty BD into AH109,and the yeast can grow in QDO(SD-LTAH) plate! So at first I thought my protein had autoactivation. But when I cotransformed my protein-AD with other protein-BD, the yeast can not grow in QDO plate. Actually I contructed about five different genes into BD vector and cotransfomed these BD with my protein-AD and all the yeasts can`t grow in QDO plate. Only the yeast containing my protein-AD and empty BD can grow in QDO plate. I have repeated this experiment for three times and always get the same results. Can my protein be autoactivated?So has anyone ever been in this situation? I am very confused.. Many many thank if you can kindly give me some advice!
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Dear Pengcheng, Have you solved the problem?
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Hello everyone, I have encountered some problems in research, I hope someone can help me. In the blood biochemical analysis of my broiler experiment, the AST (aspartate aminotransferase) of the treatment group was significantly higher than that of the positive control group, but there was no significant difference in GGT, LDH and CK. There was no significant difference in growth traits. Therefore, it seems that the treatment group did not cause physiological adverse effects. In the carcass traits, the breasts relative weight of the treatment group was significantly higher than that of the positive control group. Then can I infer whether AST can be used as a positive indicator of animal growth?
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I following the best answer.
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I am trying to run my cyanobacteria extracts in GCMS, but, the GCMS lab-solutions software is indicating that the MS communication hardware is not connected also showing code 0D80. What could be the problem and how can I overcome it?
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I suggested you to refer into the located authority dealerships of the constructive company of the apparatus namely (GCMS Shumadzu model) in the regional headquarter in your country. In addition, you could to use through the online services, the demo version and technical support of the mentioned device to troubleshoot the software or hardware.
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I need to measure hydrogen peroxide in sea water samples, out of the lab. Does anyone know a reliable and quick method?.
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Luisa María Vera , i am asking the same question as yours. i need to measure H2O2 concentration in acidified water.. have you found the answer you were aksed??? i am so glad if you would like to share here...thanks
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I must concentrate and purify a lot of dirty lysate and secreted protein samples. I just want to run them on protein gels for western blots. I'm trying to decide the best method of concentrating+purifying the samples.
I am considering TCA precipitation versus centrifugal filters.
For TCA precipitation: the pH of the sample seems problematic. I get a lot of TCA carryover. I wash 2X with acetone and yet my samples are very, very acidic.
For centrifugal filters: My samples have a lot of contaminants that I must get out. I hope I can just run fresh buffer through the filter, after running my samples. I have also heard the % loss of protein can be quite high despite manufacturer claims.
Does anyone have any thoughts on which method method is best?
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If you need your sample for electrophoresis only, then chloroform/methanol precipitation (doi:10.1016/0003-2697(84)90782-6) is your best bet. If you decide to use TCA instead, you should extract the pellet with ether to remove TCA, only neutralising it will increase the salt concentration of the sample, which may interfere with proper stacking. For safety, replace the diethylether by tert-butylmethyl ether (MTBE), to avoid the formation of explosive peroxydes. The other hazards (fire, endocrine disruptor) still need to be managed, though.
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Hello everyone,
Our lab is currently looking to purchase a plate reader and I was interested in seeing what opinions people have about some that they have used.
Some of the other labs on campus, have told us that software for the Cytation can be difficult even once you are trained and is not intuitive.
Any thoughts would be greatly appreciated!
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What sort of measurements do you want to make, and how much money can you afford to spend?
For a single-mode absorbance plate reader, I recommend the Spectramax Plus 384 (Molecular Devices). It is easy to use, robust, and has excellent photometric stability, in that the variation in the absorbance measured over time is +/- 0.0001 OD unit. This characteristic comes in very handy when making kinetic measurements with small absorbance changes. It is monochromator-based, so any UV or visible wavelength can be measured. (For far-UV measurements, you need to use UV-transparent plates, not polystyrene ones.). There is a cuvette holder, too, in case you want to use it like a regular spectrophotometer, which is very useful if you don't also have a spectrophotometer.
Here is more information.
For fluorescence measurements, I like the Pherastar line (BMG LabTech). It is also easy to use, robust, and has excellent photometric linearity. My favorite feature is that it has two detectors, allowing you to make kinetic fluorescence polarization and dual emission wavelength measurements, which is not possible on most instruments. It is rather expensive, and since it uses filter blocks, you have to buy a different block for every application. This plate reader is multimode, so it can also make absorbance and luminescence measurements. With add-ons, it can do TR-FRET and AlphaScreen, too, but the cost gets quite high.
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'Gamma GT' Biochemical analysis formula is as follows for further understanding:
Gamma GT activity (U/L) = (Δ OD/min) x 1158
I would like to know the answers to the following questions:
1. What data is to be added in the place of "Δ OD/min"?
2. Once the calculation is over, Do I apply this value in 'SPSS Software' for further analysis [To find out Mean and Standard Deviation (SD)]?
Thank you in anticipation, Sir/Madam.
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William Raja, In simple terms,
ΔOD/min = ΔOD, that is change in absorbance, divided by the total time of reaction.
Normally, yes since you are expected to have replicates.
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I observed a change in PT-INR with decreasing of Hemoglobin with the same patient
I would like to insure that results with a same cases may you have; could you refer me any papers about this topic? thanks
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I would like to label Human Serum Albumin for my experiments.
My supervisor suggested NHS and 6-Aminofluorescein as working agents.
Can anybody please suggest a working protocol?
Any suggestions on storing? Can I freeze the labelled protein in a solution?
If you have any other suggestions I would be very grateful!
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Obviously numerous examples of how you can perform the labelling can be found. It depends on whether you use the label(s) separately or as an already prepared ready-to-use sample like in:
In essence it comes down to the use of NHS in order to enable the fluorescein to get attached to your protein. Once the labelling is finished you need to rid of the excess of NHS and 6-aminofluorescein. In:
you see that they use dialysis to remove the excess of NHS and 6-aminofluorescein. In:
Bidmanova, S., Chaloupkova, R., Damborsky, J., & Prokop, Z. (2010). Development of an enzymatic fiber-optic biosensor for detection of halogenated hydrocarbons. Analytical and bioanalytical chemistry, 398(5), 1891-1898.
the conjugates (CF–BSA) were separated from unreacted dye by size-exclusion chromatography.
Your question about storage. Indeed you can make one stock solution (let say 20 mL) and make smaller portions (let say 0.5 mL) and freeze them. Once you take a portion out of the freezer you better use it one time and better not freeze it back again (to be one safe side).
Best regards.
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I'm looking for laboratories working with oxidative stress to test nitrocellulose redox permanganometry (NRP). NRP is a simple method for reductive capacity assessment based on the analysis of the MnO2 precipitate following redox reaction between KMnO4 and biological samples fixed onto the nitrocellulose. This method estimates how well the sample can give up its electrons to KMnO4, so it estimates the amount of chemical antioxidants. In other words this method can be used to measure total chemical antioxidant capacity of biological samples. Advantages of the method are: great precision and accuracy; the possibility to measure a lot of samples simultaneously; simplicity; cost (you only need a piece of nitrocellulose membrane and KMnO4). Moreover, the method can be used to obtain information on the spatial distribution of antioxidant capacity in tissue sections (both cryosections and FFPE can be used), providing unique information on the redox status of the tissue.
As the method is new, and we proposed it just recently, I'm looking for laboratories that are working with oxidative stress to test the method in their samples. We conducted thorough analyses and the method seems to be very robust. Nevertheless, I believe additional independent testing is always a good idea. Also, I believe comments of researchers closely working with oxidative stress would be beneficial for further development of this simple method.
The original paper can be found here:
A step by step protocol can be found here:
Best,
Jan
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In my opinion, there are no simple methods to evaluate antioxidizing capacities of potential antioxidants. General tests like DPPH, ABTS... only (roughly) measure the ability of the antioxidants to scavenge free radicals. An antioxidant is much more than that; it can act as a scavenger of free radicals, repair of the oxidized species (reduction by one electron transfer) or by cascade (cumulative) effect . Furthermore, the antioxidant capacity can also depend on the agent responsible for the oxidative stress conditions (selective antioxidants).I recommend the evaluation of the mutual behavior of both antioxidant and the target to be protected in every specific oxidizing environment.For details see e.g.:
  • Santos, P.M.P.; Telo, J.P.; Vieira, A.J.S.C. "Structure and Redox Properties of Radicals Derived from One-electron Oxidised Methylxanthines", Redox Report (2008), 13(3), 123; DOI: 10.1179/135100008X259231
  • Santos, P.M.P.; Antunes, A.M.M.; Noronha, J.; Fernandes, E.; Vieira, A.J.S.C. "Scavenging activity of aminoantipyrines against hydroxyl radical", Eur. J. Med. Chem. (2010), 45, 2258-2264; DOI: 10.1016/j.ejmech.2010.01.071
  • Santos, P.M.P.; SILVA, S.A.G., JUSTINO, G.C.; VIEIRA, A.J.S.C. "Demethylation of Theophylline (1,3-Dimethylxanthine) to 1-Methylxanthine: the First Step of an Antioxidising Cascade", Redox Report (2010), 15(3), 138; DOI: 10.1179/174329210X12650506623726
  • SANTOS, P.M.P.; VIEIRA, A.J.S.C.Antioxidising activity of cinnamic acid derivatives against oxidative stress induced by oxidising radicals”, J. Phys. Org. Chem. (2013), 26, 432; DOI: 10.1002/poc.3104
  • VIEIRA, A.J.S.C.; SANTOS, P.M.P. “A Tentative Classification of Antioxidants: Which Role They Play when Protecting Biological Targets from Oxidative Stress Induced Damage?”, J Med Chem Drug Des (2017), 1, 1-3; DOI: 10.16966/jmcdd.101
  • VIEIRA, A.J.S.C.; GASPAR, E.M.; SANTOS, P.M.P. “Mechanisms of potential antioxidant activity of caffeine”, Rad. Phys. Chem. (2020), 174, 108968; DOI 10.1016/j.radphyschem.2020.108968
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I want to compare the amount of an enzyme's expression (laccase for example) or presence in the tissue as a result of the experimental treatment. Is there a protein similar to an antibody that might bind with the enzyme and can be filtered then quantified by spectroscopy? or perhaps by comparison of PCR bands. I am interested to hear any other thoughts or suggestions as well. Thanks very much.
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Adam B Shapiro thank you very much for your reply and the link.
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Hello everybody,
I am trying to calculate the irreducible representation of point group 3m (C3v) for NBT (having R3c space group - 161).
Could you please give some clarification in this regard?
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the E bands are degenerate, hence there will be only a single band. So 7A + 6E is correct, summing up to 13 Raman active bands.
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Hello,
I would like to know whether there is any comparison of the ATP levels pre, during, and after exercise of different methods, intensity and duration.
Is there any research about the kinetics of ATP?
Also, what is considered as the gold-standard for measuring ATP?
Does Venous or Capillary testing more appropriate and what are the limitations?
Would love to read anything available.
Thanks alot!
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Duration Classification Energy Supplied By
1 to 4 seconds Anaerobic ATP (in muscles)
4 to 10 seconds Anaerobic ATP + CP
10 to 45 seconds Anaerobic ATP + CP + Muscle glycogen
45 to 120 seconds Anaerobic, Lactic Muscle glycogen
120 to 240 seconds Aerobic + Anaerobic Muscle glycogen + lactic acid
240 to 600 seconds Aerobic Muscle glycogen + fatty acids
The Venous testing is more appropriate
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looking for some best ref. books on Viva in Clinical Biochemistry / Biochemical Analysis / Biochemistry PDF ??
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What do you mean 'on Viva' : Viva forum?
I never heard of good books clin biochem books free available as pdf, please be more specific
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Hello everyone,
I would like to understand the interaction between my drug of interest to a protein (known). Basically, I want to study how strong the interaction is. Is there any way to measure it?
Thanks in advance,
Arun.
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Hi Arun,
As mentioned in the previous comments, there are many reliable techniques for measuring drug-protein interactions. If you don’t have the resources and equipment, then you can work together with a reliable partner to solve this problem. I know that Creative Biostructure has drug discovery-related services. This is a very professional structural biology company. I think it is very good, you can try it.
Hope it helps!
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Hi dear researchers.
I have a mixture of nanoparticles and hemin and buffers, …
It was centrifuged and washed several times.
Is there any way to calculate the residual hemin concentration?
( There are not any biological samples)
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This because table sugar is extracted naturally from sugar cane or sugar beets and hydrolyzed to glucose and fructose and never could reach the body cells in its origin form. The hydrolysis process occurs in mouth, stomach and small intestine which the products of sucrose in body may be in a similar manner to that of honey and bread. In other words, sucrose is a carbohydrate that occurs naturally in every fruit and vegetable. But, why there is no similar propaganda to the not natural synthesized chemical candy such as aspartame and so on.
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Hi there,
I think this one question is actually a combination of various different questions and assumptions.
The fact that sugar is extracted from "natural sources" such as sugar beets and sugar cane does not mean that it "good", just because of its natural origin. Likewise, you cannot say that "artificial" sweeteners are "bad", just because they are "artifical". You probably also would not say that cocain is a good thing, just because it can be extracted from plants....
In my opinion the problem is that in the modern Western diet, people consume extremely high amounts of fat and sugar. There is also an increasing use of high-fructose-corn syrup and similar products. If you buy, for example, a modern joghurt with fruit (flavour), it contains > 10% sugar. If you look at "sweets" for kids, they often contain 30% - 50% of sugar. Therefore, the "density" of sugar much higher that in fruits or vegetables.
It is probably difficult to eat so many fruits and vegetables to get similar amounts of sugar. But if you would, for example by eating huge amounts of honey and dates every day, this also would not be good for your health. At least in Europe, nutritionists warn people that also intake of too much "natural sugar" (milk products, fruit juices) can cause health problems.
You also mentioned sweeteners such as aspartam and asked why nobody is complaining about them. First of all, these products are much sweeter than sucrose or fructose, so there are much smaller amounts used. Second, there are people in both Europe and the US who warn customers not to use such products.
In summary, I would say that eating huge amounts of sugar is not good for your health, no matter if it comes from fruit, vegetables or modern "convenince foods". The peoblem seems to be that modern food is just unnaturally high in sugar and people, therefore, consume much lager amounts of sure than decades ago.
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i have been working with identification of compound by MALDITOF-MS. does this machine has the ability to quantify the amount of compound? kindly help me if there is method by which we can quantify the amount of compound using MALDITOF-MS.
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Hi Ayaz,
yes you can use MALDI-TOF to quantify drugs/metabolites. It may be a bit tricky but feasible. Provided that you have a standard calibration made using standards with same or similar chemical structure of your reference compounds (and using the same analytical conditions). The benefit especially with imaging is that you will be able to observe the actual distribution of a compound in the tissue / sample surface.
Read in this recent review article here, specifically the section: "Quantitative MALDI MSI (qMSI) of drugs: calibration, internal standards and normalization"
For more tehcnical aspects, read here:
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I have collected rats blood plasma, and serum & stored it at -4°C but the problem is that the serum and plasma have preserved more than 1 month.
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You can study mRNA expressions, they are quite stable.
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Dear Professors and fellow Colleagues,
Please I am working with corn straw biochar in CHINA and have no previous experience with. Due to circumstances I can access Google and others which has made my work daunting.
I have so far been able to find procedures to test for pH EC and the method for digestion. Please , Kindly assist me with the steps and procedures to test for these :
Total Nitrogen
Total Carbon
Available N
P
K
Ca
Mg
S
C:N
Please thank you for your time. Your help is much appreciated
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Some research manuscripts with similar objectives as yours, have described or referred to appropriate analysis protocols.
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Raman spectroscopy is a powerful biochemical analysis technique that allows for the dynamic characterization and imaging of living biological cells in the absence of fluorescent stains.
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Here is an example review of some of our recent work. Cells were fixed, for ease of study, but could also be studied live.
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We are detecting Indole acetic acid (IAA) producing actinobacteria according to Bano and Musarrat (2003) method.
The summary of the method is:-
Inoculation of the isolates in LB medium (supplemented with 0.5% glucose and 500 μg/mL tryptophan) -----> Incubation at 28 ◦C for 48 h -----> Centrifugation of the cultures at 10000 rpm for 15 min ----> 2 mL of the supernatant were transferred to a fresh tube to which 100 μL of 10 mM ortho-phosphoric acid and 4 mL of the Salkowski reagent (1 mL of 0.5 M ferrous chloride in 50 mL of 35% perchloric acid) were added ------>incubation of the mixture at room temperature for 25 min and the absorbance of pink color development read at 530 nm -----> Calculation of the IAA concentration in cultures.
Is there any method better than this one? or if any modification?
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My dear friend, the method you have mentioned is the best way to evaluate the production of auxin, but sometimes with a few changes in the method, a good result can be achieved, for example, changing the ratio of the reagent (Salkowski) to the sample (supernatant) and also adding or not adding ortho-phosphoric acid to the mix.
The incubation is also better in the dark.
Wishing you success with you dear friend
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Hi
Is there a real correlation between % of cell death and the efficiency of DNA fragmentation assay?
I want to perform DNA laddering from suspension cell sample with low % of dead cells (less than 30%) . Could it work successfully? or should I take sample with more than 70% dead cells to see clear DNA fragments? Is there a conventional threshold in this case?
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If I have data of performance of chickens, biochemical analysis, egg production traits How calculate genetic correlation and phenotypic correlation?
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can i use GENSTAT to calculate the same
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Good day to everyone.
Can somebody provide me please, to get the answer to this question?
What is the reason for the number of wells in Microtiter plate that uses in Elisa technique is 96 wells or its multiples in some cases? Nor more neither less of that.
Thank you! I appreciate the help.
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There are 48 wells in Elisa technique for small samples like in animal researches.
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What compound is used to label proteins which eventually produce the color in dip stick tests?
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I need to learn lateral flow assay can someone please share the videos for different steps of this assay as are available for other tests like PCR. I am hesitant to start my assay as I feel totally blank and have just the theoretical knowldge for LFA but no hands on training. As I am out sourcing the antibodies that are quite expensive and I dont want to waste my chemicals. Therefore please share different steps of membrane assembling, blocking of membrane, making various buffers, making colloidal gold particles and dilution as well as immobilization of antibodies on membrane. I have found few videos but that are not really helpful.
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I am working on neuropharmacological activity & want to estimate total cholesterol, glucose, and saturated and unsaturated fatty acids in rat tissue. The available kit in the market is costly. I want to know Can I did this test with the help of reagent.
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Hello, cholesterol, saturated and non saturated fatty acids is cheapest possible way to analyse with good accuracy is by GC-FID. For glucose you can use different methods such as titrimetry, spectrophotometry or by HPLC wit refractive index detector.
Hope this info will help you.
Good luck!
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I want to determine the fluoride content from egg after boiling for 3 minutes. Is there any calorimetric method for determination of fluoride?
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I found this article fragment that reviews methods of fluoride determination. It appears to come from a US government publication. Unfortunately, the full references are missing.
The fluoride ion-selective electrode (ISE) seems to be the most common method.
Here is a Wikipedia article about the fluoride ISE:
You would have to make an aqueous extract containing the fluoride to use this method.
Here is a commercial fluoride ISE:
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The katal is the SI unit of catalytic activity (http://en.wikipedia.org/wiki/Katal). It is the amount of enzyme or other catalyst required to produce 1 mole/s of product.
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Following
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Hi everybody!
I'm working with RNAi in Setaria. The transformation that I'm working affect the central metabolism. I'm performing qPCR analysis to select the events for biochemical analysis. My questions are:
1. Which is the minimum number of reference genes that I should test?
2. Should I use one or more RG to perform the expression level calculations?
3. In my case which method is more reliable Delta Delta CT or PFAFFl
Thank you!!
Camila
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Hi Camila,
you got already very valid suggestions from other researchers.
However, the number of reference genes that you will use depends a lot on your organism too. I do not work with plants, but for my experiments it was impossible to go for one reference gene alone... I tested many of them, spending a large amount of time, but I could not find any RG stable enough to stand alone. Therefore I went for 2/3 RG.
I also like to test at least 6 or 7 reference genes before deciding on which to use... it takes quite a large amount of time, but it makes your work more solid and it will be less stress once you try to publish your results (I can attest that almost all reviewers will question if you followed the MIQE guidelines!).
Hope it helps!
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Hi, I am trying to measure superoxide levels using EPR with DMPO as a spin trap. I had tried in isolated mitochondria and I got nice spectra (only in presence of inhibitors). Now I like to use total tissue, kidney and heart. If any of you have tried this can you provide conditions such as buffers and  how you homogenize the tissue.
Also, anyone has experience in injecting spin trap into animals  and measuring EPR later ? Ideally I want to perform in vivo measurements, or something close to that.
Thank you 
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I trapped nitric oxide and I've got many remarks and observations.
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Hey,
1) I am performing MTT assays and was wondering how much the cell size can influence the mount of metabolized MTT?
I thought that the amount of mitochondrial membrane, (so also the amount of active enzymes that metabolise MTT) correlates with cell size and therefore lets say 100 normal sized cells could metabolise approx. the same amount of MTT than 160 smaller cells, right?! 
2) does anybody know if and how the metabolism of nutrients (Glucose, aa ) is connected to the activity of the MTT metabolizing enzymes ?
As maybe the presence of nutrients at the time point of the addition of MTT !!! can influence the capacity of metabolizing the chemical .....  (I mean : 100 cells consumed a lot glucose --> remaining glucose in medium is less and metabolism goes down...so also the metabolism of MTT, ..... smaller signal,.... but treated cells, where only 50 are present consumed less Glu, therefore still more in the medium when adding MTT and therefore 50 cells can metabolize more than 50% of the MTT than 100 untreted cells) 
Thanks a lot for reading and trying to understand and helping :) ! 
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what is the interpreation of increaseing of decreasing metabolic activty?
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Coating proteins of lipoproteins.
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Dear Heera Ram,
A good alternative to the ELISA method, can be the classical radial immuno diffusion (RID) or turbidimetric assay on microplate, both made in house at low cost as reported below.
Apolipoprotein A-I A-II and B determination by RID
Reagents
Gel agarose A-I and A-II: mix 400 µl of antibody from rabbits anti apolipoprotein A-II with 20 ml of 10 g/L agarose solution containing Tris-barbital-lactate buffer at pH 8.6 (dissolve 0.045 mM Tris, 0.015 M barbituric acid, 1.9 mM NaN3, and 0.21 mM Ca-lactate)
Gel agarose B: mix 10 µl of antibody from rabbits anti apolipoprotein B with 20 ml of 10 g/L agarose solution containing Tris-barbital-lactate buffer at pH 8.6 (dissolve 0.045 mM Tris, 0.015 M barbituric acid, 1.9 mM NaN3, and 0.21 mM Ca-lactate)
Procedure
Dispense in 3 mm diameter well of agarose plate, 5 µl of diluted serum sample (1:50 for A-II and 1:3 for B) in 0.15 M NaCl, are dispensed and incubate for 5 days for A-II and 72 h for B at room temperature. The ring diameters were measured after staining with Coornassie Blue R.
Apolipoprotein A-I, A-II and B determination by turbidimetric on ELISA microplate
Diluent antiserum: dissolve in Tris-HCl buffer 8.0 mM at pH 7.4, 3.5% (w/v) polyethylene glycol 6000, 1.9 mM NaN3.
Procedure
Working in duplicate, dispense in microplate 200 µl of anti-human apolioprotein A-I, A-II or B, diluted 1:11 in diluent antiserum buffer (dissolve in Tris-HCl buffer 8.0 mM at pH 7.4, 3.5% (w/v) polyethylene glycol 6000, 1.9 mM NaN3), and incubate at room temperature for 20 min. Then, dispense 20 µl of 1:60 diluted serum sample in 0.15 M NaCl for A-I, and 30 µl of 1:60 diluted serum sample in 0.15 M NaCl for A-II , while dispense 30 µl of 1:30 diluted serum sample in 0.15 M NaCl for B, mix and incubate for 90 min. for A-I and A-II and 120 min. for B, at room temperature. After careful shaking of the dish, turbidity was measured at 340 nm against a basic value (200 μl of anti-human apoliprotein A-I or A-II dilution with respectively 20 µl or 30 µl of 0.15 mol/1 NaCl).
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.
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Try dragendorff's reagent and vanillin in sulfuric acid.
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Dear all,
I would like to know how soil amendments (e.g., lime, wood ash, EDDS, EDTA) improve tree physiological parameters such as CAT, MDA, SOD when plants grow in contaminated soil. How these parameters help to improve metals accumulation in plants? How soil amendments improve metals accumulation in plants?
Thanks for your help.
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Do you mind sharing privately with me please?
Thanks
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I would like to draw a DNA structure (both single strand and double strand).
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Hi,
"Avogadro" is a software that you can easily download and build your DNA and then save in PDB format
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Hi everyone,
I want to perform a cellulase activity assay using industrial cellulase and industrial cellulose (microcrystalline cellulose). In case of cellulase produced by the hydrolytic microorganisms, the crude fermentation broth (centrifuged/filtered) containing cellulase is mixed with the cellulosic substrate in appropriate buffer solution, incubated and then analyzed.
The industrial cellulase comes as a solid substance. So, when this cellulase is to be used for the same assay, should it be prepared as an enzyme solution using the common buffers (acetate, citrate, phosphate)? If so, then is there any protocol for preparing the enzyme solution and using the same for the assay? What are the major affecting factors and their optimum conditions in cellulase activity assay?
Regards,
Shiladitya
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Hi Ana,
Thank you for your response. I will use some different substrates for the assay. I will also use CMC, by the way. Actually my question is, how to prepare the enzyme solution using the solid enzyme power, which is a protein. Should I use sterile distilled water or a specific buffer with a particular pH? Does this affect the activity of the enzyme?
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What physiological/biochemical analysis can be carried out on seeds that would be of scientific benefit?
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It also depends on what kinds of seeds you want to look at. Some have not been studied at all so there is all to discover; others are already well researched in terms of their composition and properties.
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what is the diffidence between case-control study and cross-sectional study?
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In cross sectional study exposure and outcome are present at one time no follow up is needed
and we can find out Only prevalence in cross sectional studies
while in case control study cases and control groups are assigned and they are followed up for the particular risk and outcome and we calculate odds ratio relative risk attributable risk and hazards ratio and find how much lethal is effect of risk of outcome
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I am using formula for this FFA%=(v-b) X N X28.2/w. Is this correct or not?
Can anyone suggest a formula?
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Dear Sir,
Try using a simple method called "Isopropyl Alchol Method".
You simply add 1ml of oil with 10ml of IP Alcohol and few drops of phenolphthalein indicator. Titrate this mixture against 0.1N NaOH until pale pink color last longing for 10 sec appears. Note down that as your end point and That's your acid value.
Its very simple and more reliable. This method helps in giving you your oil's acid value directly and FFA through a simple relation.
FFA % = Acid Value/2
Good luck with it
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Hi! Working on microbiological methods for an undergraduate thesis project. Wondering how detailed we have to be identifying the bacterial isolates we have in order to have respectable and meaningful data.
We aim to identify potentially pathogenic bacteria from holy water fonts in churches. We'll do so by collecting holy water samples from the fonts, then inoculate them into selective media.
We're focusing on Streptococcus and Staphylococcus-- so we're inoculating the diluted samples into Mannitol Salt Agar (selects for Staph) and (selects for Strep). So with these media we narrow down the bacteria to the genus level. For a meaningful study, do we have to identify all colonies up to the species level?
Initially we planned to do this via DNA sequencing of colonies, but it proved too costly. What biochemical tests should we focus on to differentiate the Strep species and the Staph species, while reducing costs/redundancies?
We're thinking of Catalase Test, CAMP test, Taxos A and P tests for Strep; and Blood Agar plating, Coagulase Test, and Catalase Test for Staph. Would these be enough to identify the species under Streptococcus and Staphylococcus? Other suggestions of other tests that would simplify the identification would be much appreciated.
Thank you very much!
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For Staph and strepto a wise choice is to use API
API Gram positive Identification
  • API Staph – Overnight identification of clinical staphylococci and micrococci
  • RAPIDEC® Staph – 2-hour identification of the commonly occurring staphylococci
  • API 20 Strep – 4 or 24-hour identification of streptococci and enterococci
  • http://www.biomerieux-usa.com/clinical/api
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I want to do water and ethanol extraction by an inhibition assay, in which I need to dissolve the extract in 0.5% DMSO. 
Can any one help me with the steps? Thanks.
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1- First, a Beaker or a crucible should be brought, weighed (Assume that the weight is 100 g)
2- Transfer the extract to the Beaker
3- The solvent used in the extraction process shall be disposed of by evaporation of until the dry matter is obtained as far as possible
4- The beaker is weighed after full evaporation of the solvent (Assume that the weight is 110 gm)
5- The weight of the extract (the weight of the beaker with the extract - the weight of the empty beaker) = 110-100 = 10 g
6- The extract is dissolved in the appropriate solvent Ethyl alcohol is often used and an emulsifier may be added (the amount of the solvent is calculated to obtain the desired concentration(
To prepare different concentrations:
1- The extract is dissolved in the minimum amount of suitable solvent and then a quantitative transfer is done to a volumetric flask with a final size of 100 ml (the appropriate size for the quantity of the extract).
The concentration of the extract is calculated as follows
10gm/100ml = 10×103mg/100ml= 100 mg/ml
Different concentrations could be prepared from that stock solution
To prepare 5 mg / ml with a final volume of 100 ml
V1×C1 (before dilution) = V2×C2 (after dilution)( the concentration which we would to prepare )
? ×100 = 5×100
V1= 5×100/100= 5 ml
Take 5 ml of stock solution (Conc 100mg/ ml) and supplement with appropriate solvent to 100 ml in volumetric flask.
To prepare 0.5 mg / ml with a final volume of 100 ml
? ×100 = 5×100
V1= 0.5×100/100= 0.5 ml
Take 0.5 ml of stock solution (Conc 100mg/ ml) and supplement with appropriate solvent to 100 ml in volumetric flask.
In that case we use a DMSO 0.5% instead of the solvent
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which protocol best suit for the isolation of endophytic microbes and their enzymatic activities test. and how to confirm second we got new microbes not present the first isolation time.which is the easiest way to microbes identification?
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This article will serve your purpose...
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According to psychological research, permanent anxiety with adrenaline secretion damages DNA and causes abnormalities. Can this be scientifically verifiable?
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thank you for your answer,
How Does Stress Affect Cancer? Can we control the spread of cancer by controlling stress?
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Does anyone know of a method that can reliably deplete all hemoglobin-bound and free oxygen content of the blood ex vivo? I need to create a sample of oxygen free blood in a sampling tube or syringe. It does not need to be "life compatible", since it will not come into contact with a living system again, however it is necessary that all oxygen content is removed.
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Try to use Carbonmonixide or any other substance that dispalces teh oxygen from the hemoglobin.
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Now looking in detail of each blood source and develop correlation among mosquito preferences and blood source.
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thanks Abhijeet and Khalid for your suggestions. i will look in detail of each, LCMS and Spectrometery.
Cheers , Have a good day
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Actually i wanted to asked if I carryout detailed Biochemical profiling study by means of TPC,TFC, DPPH,TOC, redcuing power, antimicrobial, mic, ames, hemolytic , dna damanging study on natural extract but without HPLC , lc-ms and gc-ms .. Is there probability for my work to be published in good journal?
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if you already have the title and abstract for your article, you can use the following tools from Elsevier and Springer to help you pick a right journal among those that belong to the respective publisher http://journalfinder.elsevier.com http://journalsuggester.springer.com The output of these tools shows inter alia average article processing times and impact factors of the journals.
Once you make a short list of potentially suitable journals, you can check whether they are covered by Scopus here https://blog.scopus.com/posts/titles-indexed-in-scopus-check-before-you-publish and by Web of Science here mjl.clarivate.com
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How to estimate iodine value from fats and oil samples?
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by using Wijs Method. 
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This machine seems very cheap for semi automated analysis so I wondered if anyone had experience in a research setting?
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Im sorry ,Idont use it
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Can it help to understand adaptive strategies of them?
Any idea?
Thanks for your answers 
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The conditions in the different geographic areas are clearly different, this causes that the same taxa undergo transformations that can be both morphological and physiological, this is used in studies related to the adaptability that is able to develop a certain organism before different conditions, which Tells us its ability to survive under unequal conditions, and in case of possessing any component that can be exploited, such as pigments, it is possible to extrapolate the conditions of the environment where it produces to be exploited later.
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A researcher ask me and my Italian colleagues about the topic in the question string, providing the following statements. Anyone can help me answering him?
Since the Nobel prize was awarded in 1977 to Rosalyn S. YALOW for the development of new methods of biochemical analysis that make it possible to measure insulin concentration in human plasma, these methods have been used worldwide. In 1981, the monograph „Diabetic Coma: Ketoacidotic and Hyperosmolar“ (SCHADE et al.; University of New Mexico Press, Albuquerque) was published and on p 67, Figure 6.3 has the names of 12 authors who have reported sufficient amounts of plasmatic insulin in patients with DKA. In contrast, absolute deficiency of plasmatic insulin has been reported in diabetic patients with hyperglycemic hyperosmolar nonketotic syndrome (e g, VINIK et al: Lancet 2:1970;797-9) as weĺl as in diabetic patients on routine control without subjective complaints (e g, MATSUYAYAMA et al.: Hormone Metabolic Research 7:1975;452-6).
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Is there any reliable method other than mass spectrometry ?
Cholic Acid
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There's the enzymatic kit, but it only measures total BAs. For each BA species the best method is tandem mass spectometry 
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Hi,
I am looking for C57/BL/6 mice (8-10weeks age) blood plasma biochemical parameters, i.e., blood urea, ALK, GOT, GPT, cholesterol, triglycerides, HDL, LDL.
I need these data as control mice data.
Thank you,
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A good place to start looking is the Mouse Phenome Database at phenome.jax.org
From the MPD main page, click on "Phenotype" and browse the blood measures, or click on  "Strains"  and follow the top links on the next three pages to get to the available phenotypes for C57BL/6 mice.
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I've been using milk clotting units assay to determine the activity and stability of bromelain fraction in artificial stomach juice. What I'm still wondering and not getting, is why do I have to add drops of toluene on milk substrate? According to Balls and Hoover (1937), the milk substrate when not used for ~4 days must be kept under toluene in refrigeration. Following the assay as described by Enzyme Development Corporation, toluene was added to the substrate after it's fully dissolved in buffer acetate, before filtering through glass wool and subsequent refrigeration. So, what's the use of toluene and how did it works?
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antiseptic
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I can not get back to grow up my MDA-MB-436 cells after freezing in liquid nitrogen tank.I used 7% DMSO with FBS for freezing medium. But when i do thawing again my cells, they didnot alive again.
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My advisor advise to me to use 7% DMSO, the problem occured only in MDA-MB-436 cell lines only , so I have idea to change the DMSO % from 7% to 10%, Thanks for your Suggestion Sister Nguyen Tu,,,,, Dear Magdalena Matysiak,,I cant solve this problem.
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