Immobilization - Science topic
The restriction of the MOVEMENT of whole or part of the body by physical means (RESTRAINT, PHYSICAL) or chemically by ANALGESIA, or the use of TRANQUILIZING AGENTS or NEUROMUSCULAR NONDEPOLARIZING AGENTS. It includes experimental protocols used to evaluate the physiologic effects of immobility.
Questions related to Immobilization
I am working on immobilization of peroxidase on magnetic nanoparticles using adsorption. Unfortunately, the change in enzyme activity is very low. Consider the absorbance change over 3 mins for the immobilized enzyme:
And this change for the soluble enzyme:
So, please what the reason behind that difference and how to fix it, given that I have varied several factors like pH, temperature and [Enzyme] but alas with same consequences.
Hi, I have always done my in-vitro experiments of protein-antibiotic interaction at a pH of 5.5. Now that I want to do some experiments with the SPR, is it still advisable to use this low pH? Thanks!
I am working on immobilization of peroxidase on magnetic nanoparticles, I want to study the influence of immobilization on pH, Temperature and kinetics of the enzyme. How to do so given that the immobilized peroxidase get precipitated after immobilization?
I have a material supporting a peroxidase enzymes and I wish to collect the infrared spectrum of the complex support-enzyme, but this system is in buffer medium (citrate-phosphate). The technique available for FTIR analysis is by KBr pellet therefore what is the pre-treatment useful to dry the support with enzyme without degradation of biomolecules attached?
I am trying to perform covalent immobilization of streptavidin protein on glass surface. This is done by first coating the glass with 2% APTES-toluene and then with 2.5% glutaraldehyde-water solution. Then I add the streptavidin which is in PBS (pH 7.4) on the glass coverslip. This doesn't seem to work. Please let me know the right pH, salt and temperature conditions that are appropriate for the reaction between glutaraldehyde and amine groups created by APTES coating on glass.
Some enzymes have high immobilization efficiency at acidic medium while others prefer basic medium or neutral medium. why?
I want to know when we use gold electrode and immobilize thiolated aptamer on the gold surface later with living bacterial cells after incubation with 2 concentrations of bacteria I have worst results. How to optimize it?
Chicken or Egg?
Considering the outcome of 183 patients admitted to Tongii Hospital in Wuhan in January, mean age, 54 when all patients received supportive care and antivirals. 41% had comorbis chronic diseases. 45.9% remained as inpatients with an overall mortality of 11.5%.
The patients were tested for prothrombin time, activated partial thromboplastin time, antithrombin, fibrogen, D-dimer and fibrin degradation products every 3 days for the first 2 weeks as inpatients. 71.4% succumbed to the virus as non-survivors and 4% showed no evidence of disseminated intravascular coagulation.
Speculation as to whether this is caused by the virus directly has been presented in the news bulletins giving COVID 19 an even more sinister characteristic or may the observed blood clotting be more due to the comorbidity conditions with a pre-existing thrombophilia tendency, than purely COVID 19. A chicken or the egg discussion of this situation needs to be addressed.
Thrombosis can simply occur due to immobility, particularly postoperatively and, although patients are regularly turned intensive care treatment, this level of activity may exacerbate blood clotting complications. Clearly pre-existing cardiovascular conditions are an important factor such as arterial thrombi in MIs and Strokes.
Genetic factors that interfere with the human coagulation cascade are relatively common. Thrombophilia can be caused by a severe deficiency of inhibitors (type I) or a severe elevation of coagulation factors the can be congenital or acquired also arterial, venal or combined. Venal thrombosis can be portal, renal, hepatic, Paget-Schrotter disease (upper extremity) and Thoracic outlet syndrome (unrelated to trauma).
Of the congenital conditions 5% of the population have the Factor V Leiden thrombophilia condition where 95% carting this genetic mutation develop a blood clot during their life.
• Prothrombin mutation (G20210A, 5’UTR)
• High homocysteine levels due to MTHFR mutation
(High homocysteine levels also due to vitamin deficiency B6, B12 and folic acid)
• Factor VIII promoter polymorphism (high FVIII levels)
• Other factors causing blood clotting are autoimmune disorders such as Anticardiolipid antibodies
• Lupus anticoagulants
• Renal disease (renal loss of thrombin)
• Budd-Chiari syndrome
Some rarer coagulation abnormalities include
• Plasmogen and fibrinolysis
• Paroxysmal nocturnal haemoglobinuria (haemolytic)
• Protein C deficiency
• Protein S deficiency
• Antithrombin III deficiency
Lillicrap D. Disseminated intravascular coagulation in patients with 2019-nCoV pneumonia. J Thromb Haemost. 2020;18(4):786‐787. doi:10.1111/jth.14781
If I found increase in total distance traveled and reduction in immobile time in open field test with enhanced hippocampal weight can I conclude normal anxiety which is helpful.
In addition, is there is a relation between reduction of Erk, myc, miRNA and serotonin and reduction in anxiety?
Thanks and best regards.
I'm working on a manuscript right now that needs a meta-analysis. In articles that show a percentage change in the mobilization of heavy metals, I wish to do a meta-analysis. However, I'm unsure if a metanalysis using percent change is really feasible.
Some polymers like polycarbonate, polysulfone, polyetherimide are highly hydrophobic. is it possible to immobilize streptavidin on these polymer surfaces?
I am performing esterification reactions with immobilized lipases on epoxy supports. During the first reaction everything goes as expected, achieving great yields of fatty acids to biodiesel conversions. However, during the second batch/cycle there is a huge decrease in the yield of reaction. The lipases are covalenty bonded to my support as I could check with some techniques; so, the explanation may be that the immobilized enzyme is lossing its activity. What could be causing that? After the first reaction, I filtered and washed the support with ethanol and later with my buffer solution and I performed my reactions with ethanol.
Thank you for your help!
Hi! I am trying to measure the potential nitrification rate (PNR) using the "shaken soil slurry method", following one from Drury et al. 2008. Because of sample limitation, I scaled down the sample and working solution amount to 6g and 40mL. In the past I tried it without shaking the samples during incubation but of course I got useless results with negative PNR. So I tried using a rotary shaker this time. Here is what I did:
1. After putting the soil sample and working solution (made according to the protocol above) in a 50mL tube, I shook the mixture vigorously.
2. Immediately I took the initial 15mL of the aliquot for t=0.
3. I put the rest of the tube on rotary shaker at 200 rpm for 24 hr incubation (I also transferred couple of samples in 125 mL Erlenmeyer flasks, also shaken, for comparison)
4. I added few drops of flocculent solution (CaCl2 and MaCl2) into the aliquot and it was centrifuged at 3000 rpm for 5 minutes and the supernatant was filtered using filter paper
5. The filtered solution was analyzed in SmartChem for NH4 and NO2+NO3
6. After incubation, 15mL of the incubated sample was processed as 4 and 5.
I know that I should have taken multiple samples along the incubation to do linear regression but I am short on materials. After all this, I compared the results among control (no rotary shaker), 50 mL tube incubation, and 125mL erlenmeyer flask incubation. I was expecting some notable decrease in NH4 and increase in NO3 with the later two, or at least the flask samples. However, I see that NH4 did not decrease consistently (some even increase with incubation) and NO3 content even decreased for one of the flask samples. I am really confused why the results would come out like this. Here are my thoughts:
1. SmartChem measurements are being inaccurate? I do see that the NO3 levels are quite low compared to the standards used in SmartChem. Maybe this is creating some inaccurate measurements?
2. Perhaps rotary shaking falcon tubes is not enough to create aerobic conditions throughout the sample, thus leading to denitrification. However, this does not explain why I saw decreased NO3 with one of the flask samples which should have thoroughly aerobic condition.
And here are my main questions:
1. Why would NH4 levels increase with incubation? My understanding is that the conditions of PNR assay should only decrease NH4 via nitrification and immobilization.
2. Is there a way to salvage PNR results riddled with negative PNR? I think negative PNR occurs due to either insensitive measurements or denitrification and NO3 immobilization during incubation. Is there a way to account for the latter possibility in my data?
Can anyone offer to explain???
The concept of immobility is showing up -- and often in relation to the closures that the pandemic has created. My concern or interest is in the way immobility is used. Often it seems posited as the opposite of mobility (or in other words NOT migration) and that is rather narrow. Immobility is also used to describe the limits on peoples who would otherwise cross national/international borders. Shouldn't internal movement factor into our discussion as an alternative? And immobility is more than not migration, would be interested to hear thoughts on this.
An enzyme is immobilized on multiwalled carbon nanotubes (MWCNTs) which were magnetized by filling them with Fe3O4 nanoparticles (to prepare magnetic MWCNTs) . The immobilized enzyme was used to catalyze an acidolysis reaction of a fat with Oleic acid. I was wondering if the Fe3O4 nanoparticles of the enzyme support may get involved in oxidation of the unsaturated fatty acids present in the reaction.
Recently, the immobilization of β-D-Glucosidase on Fe3O4@SiO2 magnetic nanoparticle has been carried out in our lab. The Fe3O4@SiO2 was modified with 3-aminopropyl triethoxysilane to obtain amino functionalized nanoparticle,then activated with 2 % (v/v) glutaraldehyde according literature. However, the immobilization efficiency of β-D-Glucosidase protein is relatively low(~10%),leading to very low enzyme activity. Can someone show me some advice to improve the immobilization efficiency?
Protocol on soluble carrier material selection for coating bacteria in order to rapidly reach bottom of ETP for wastewater treatment.
i want to know about the ways glucose can be supplied to the system where glucose oxidase is immobilized so that the system becomes stand-alone. kindly help!!
I'm working with enzyme immobilization on magnetic supports and I can't find specific protocols for characterization of these supports and enzymes after immobilization by microscopy.
I am working with enzyme immobilization. I made the immobilization using 10 mg of support with 23000 Units/L of activity, then I recovery from the supernatant almost 70000 units, so my immobilization yield is almost 71 %. Now I want to determine the storage stability over a time period but I don’t understand the protocol. What I did was to storage the immobilized solid suspension at 4 degrees and then I determine the activity every 4 days. But for example, first Activity of the suspension was 5 U/L, then 8, then 10, then 14… how do I determine the storage stability using a relative residual activity?
After the immobilization of the biomolecules, the value of ks changes due the change in electrochemical peak current. In that case what exactly can be interpreted by this change?
Hi Dear Friends
I immobilized CuO on the surface of CNT via precipitation method.
First I want to know that whether or not CuO functional groups would react with functional groups of CNT? I mean O with O=C-OH?
Or this synthesis just has a physical nature and no new bonds between two materials would form during this immobilization.
Second, I would like to know that except for NMR which can successfully demonstrate this synthesis, whether FTIR can be reliable to show this reaction (if would be)?
I cloned a bacterial protein (19kDa) in pET15 vector, with 6x his tag. After overnight induction at 30 degree C, I sonicated the cells and purified the protein on fresh NiNTA column.
After immobilizing the protein onto the column for 15-30min at 4 deg C, I wash the column 5 times without imidazole (protein got eluted during wash with 20uM imidazole in pilot expt). Even though my last wash is clean, as soon as I add 100uM imidazole, I see proteins start to come out of the column, everything gets eluted by 300-400uM imidazole. Surprisingly I see more than 10-12 bands in my 100uM imidazole eluate, ~5 bands in 200uM eluate and 2-3 bands in 300uM eluate. The intensity of my protein also decreases with each eluate, hence I cannot use the subsequent eluates for my assay.
we are currently working on the cultivation of the microalgae Dunaliella tertiolecta. We try to count the cells in a Thoma cell counting chamber under the microscrope. Problem is, the cells move phototactically, thus the counting of cells is inaccurate at best, caused by rapid movement of the cells under a light source.
I'm wondering if anyone knows of a method to immobilize the cells? I'd be very grateful for any suggestions!
Best regards and thanks in advance,
there is the same commercial protein from two different vendors which use two different descriptive method about receptor-ligand affinity. I can't understand the "linear range", what is the mean.
1. When Recombinant Human SIRPa/CD172a Fc Chimera is immobilized at 2 µg/mL, Recombinant Human CD47 binds with an ED50 of 0.04-0.2 µg/mL.
2. Immobilized Human SIRP alpha, Fc Tag at 5 μg/mL (100 μL/well) can bind Human CD47, His Tag with a linear range of 6-100 ng/mL.
WE all know that POM could be immobilized by incorporating them in pores of MOFs? Could we do the same thing with the substituted POM or lacunary poms also? Please suggest some readings.
A.o.A everyone . i need your suggestions.
I want to work on cadmium immobility by the use of nanoparticles and biochar. In already cited literature the work has been done on wheat and rice plant .use of Zno and Feo nanoparticles with plant based biochar. foliage spray of nanopartciles on plant and biochar application to soil for plant roots. now can i work animal based (manure bichar) instead of plant based biochar? New plant species to work. i want a novel topic for my PhD research work.
Need your suggestions .
I've been trying to use 5.5 cp and 45 cp Sodium Alginate for microbial entrapment but the beads are getting fragmented in pH 7 and above. In pH 6, however, they are kind of stable. I have tested with blank alginate beads for all the cases.
I maintain the pH of the media with NaOH and HCl.
And my growth media is mineral salt media which is a minimal media. Carbon source is phenol.
The beads are made from a stock solution of Sodium alginate which is in the carbon free MSM media. And the CaCl2 is made in de-ionized water.
In one reaction, cyanamide and 1,6-diaminohexan were used to link one compound with the NH2 functional group and the other with the COOH. I do not understand exactly the role and function of cyanamide and 1,6-diaminohexan. Can anyone help me?
I am trying to develop a uPAD that is similar to wax printed paper based ELISA techniques that have been developed.
However, I noticed that such devices are based on sandwich ELISA by immobilizing an antibody in the test zone as the analyte is then an antigen. I seem to understand antibodies adsorb well (are immobilized well) on paper.
In my case, I want to perform an indirect ELISA such that an antigen would be immobilized in the test zone. After which blocking / washing would be done before adding the sample (containing an antibody which would be the analyte in this case), washing, and then adding the substrate for the colorimetric reaction.
However, I am having difficulty finding information on whether antigens can be immobilized effectively on cellulose; will they be dislodged from the test zone when applying wash and different solutions when running the test?
I appreciate any help on this matter.
I have flat substrates (2 mm x 2 mm) ready to be coated with biotin and then streptavidin. I do have a protocol for such functionalization but only for microfluidic channels. Does anyone have a better idea to coat the surface of flat-square slab other than dipping the it into reagents? Thanks in advance!
I am monitoring the degradation of contaminants using immobilized enzymes on carbon support. However, to complete the mass balance of the degraded reactant, I have to perform a mass balance on both the solid and liquid phases. Is there a method for solid-phase extraction (SPE) that can extract the degradation reactants and products without affecting the immobilized enzymes? Previously, I've used vortexing for SPE (for other types of experiments not involving enzymes) but think doing so will also remove the enzyme. Any suggestions are greatly appreciated.
I have a large amount of gold wafers each of them bearing immobilized silica nanoparticles of either 200 or 50 nm size. I would like to reuse them as they are extremely expensive. Any idea of how could I remove them?.
Thank you in advance
I have immobilized an enzyme on the immobilization resin Dowex. How can I determine the number of enzyme units present in the powder form. Is it possible that enzyme assay is performed with powder and enzyme units are reported in units/g instead of units/ml. For example, to perform laccase enzyme assay, 10μL enzyme sample is required and results are reported in units/ml. What if I take 10mg of sample and report the results in units/g by performing the same procedure. If it is possible, then kindly provide the reference document or any other way to perform enzyme assay on powdered immobilized enzyme.
Dear community, I'm looking for at least one article, where the chemical immobilization of a ex situ obtainedMOFs over textile fibers is reported. The most of papers report the in situ synthesisand growing of the MOFs onto the textiles, I need a report of MOF produced separately, and then anchored over the textile fiber.
I would really appreciate if you can help me, even by telling me there's no article of this issue.
I'm using the commercial GOx activity assay from Sigma Aldrich. I'm testing both commercial GOx just dissolved in PBS and GOx immobilized on my electrode nanomaterials. The absorbance at 570nm peaks at abs value over 1, and it declines over time. I thought the absorbance would increase as more H2O2 is produced then plateau to stay at a high absorbance level? When I took out the plate after the reading, and the hot pink color has turned fainter. Anyone have any insight on why/how this happens? Could something in the well have reacted with the dye and turned it back to the reduced form??
I am working on heavy metal bioremediation using bacterial isolates. I have immobilized bacteria in 2% sodium alginate then cross-linked in 0.2M calcium chloride for 30 min. I have successfully prepared calcium alginate beads with a diameter of approximately 2.0 mm. These alginate beads were used in a carbonate-bicarbonate buffer (1mM) at pH 9.2 for the heavy metal biosorption. But I have observed that the beads were started to degrade within the 2 days in the buffer. Is there a way to improve the stability of the beads or any other method to immobilize the bacteria for treating the alkaline waste? I need to do biosorption studies in alkaline environments.
I want to know what is the most cheap and simple immobilization method that are suitable for biodegradation of wastewater from leather industry, that are polluted with lipids (in lab scale). And i also want to know the most suitable carrier for the method (in lab scale).
We are aiming to bind streptavidin to polyacrylamide surface. The EDC/NHS method bounced on me as a common method, utilizing the -NH2 of polyacrylamide and -COOH of streptavidin. Is there any unconsidered factors that may block this route? If EDC/NHS is viable to immoblise streptavidin to acrylamide, how should the reaction condition be set? Consider the static charge of polyacrylamide and streptavidin ( isoelectric point = 6), which pH is optimistic? Should we use a 2 step EDC/NHS xlk or 1 step?
i am performing SPR experiment and i am referring some journal and websites they stated regarding coupling buffer and immobilization buffer so ihave confusion about these buffer.
Dear colleagues I need some tips about the immobilization of laccase enzymes. I am currently planning to immobilize it in magnetic mesoporous nanomaterials, but I would need some advice on how to proceed to bind the protein to the support.
in advance, thank you very much for your help
Hi to all I immobilized a peroxidase on a new synthesized MOF. The reviewer of a journal paper asked me to consider the inhibitory activity and specific affinity of my immobilized enzyme in the introduction. How I can answer this comment of the reviewer for a journal paper revision? What does it mean? In my opinion, these items are related to biosensors. I reported the influence of immobilization on km in my article but I have no idea about the inhibitory activity.
Dear research community.
I want to study FTIR spectra of Immobilized enzyme on alginate beads before and after biodegradation, do i need to grind the Immobilized enzyme on alginate beads for the said analysis.
A quick response is needed.
Thanks for your attention.
Hi, I am going to study the DNA1(21mer) bonding to DNA2(21mer+aptamer conjugated to it(42mer)) through EIS. DNA1 is immobilized on the surface of my gold working electrode through thiol group affiliation to gold.
I am applying EIS in each immobilization step. based on the literature in each step, the Rct increases. But in my case, in DNA2 to DNA1 bonding step, it decreases. Does anybody know what will be the problem?
I immobilize fluorescent peptide on chitosan films and when I try to measure the thickness of the film with ellipsometry, the software says that I have a film with 2 nm or less. However, with chitosan films without immobilization of the peptide, I detect a thickness of 20 nm.
I already tried to change the model but it did not work. Is it possible that the fact of the peptide has fluorophores interferes with the measurement? Is it possible that the peptide is absorbing the wavelength?
Thank you so much!
I want to investigate protein interaction by SPR. I want to do amine coupling for ligand immobilization on-chip surface. first, activation of the surface by NHS/EDC, and then injection of the ligand should be done. based on chemistry, activation of carboxymethyl surface by NHS/EDC should be done at pH 4.5-7.2, and the reaction of NHS-activated molecules with primary amines of the ligand is most efficient in pH7-8 (Ref: Thermo scientific), but in the SPR instrument book (Biocare) mention ligand immobilization by amine coupling should be done at pH 1 unit lower than the isoelectric point of ligand due to electrostatic interaction toward the carboxymethylated surface. I get confused! which pH should be set for ligand immobilization?!
Actually I have faced a significant quantity of nanocatalyst loss during immobilization on glass surface. Though I have used ethanol(volatile) to spread the catalyst effectively towards the surface of a glass but somehow found significant drop of catalyst outside the glass.
Is there a simple (that is one that requires few and not very exotic reagents) chemical reaction to "activate" or "functionalize" the polystyrene of a simple microtitre plate?
In other words, I would like to add carboxyl groups to the surface of a common ELISA plate to then use ethyl-carbodiimide hydrochloride and N-hydroxysuccinimide to immobilize a target on the bottom of the well.
I am doing immobilization of amylase from sodium alginate, beads does not form properly and they are not become hard or melted when separated from calcium chloride solution. please guide me how can i improve my immobilization protocol.
The soils which are haiving high C:N ratio will be beneficial for agriculture or not. Here i want to know the what is the ideal C:N ratio of the soils for better crop growth & yields.
I am planning to perform an antibody-ligand interaction study with SPR/Biacore. The idea is to immobilize my antibody with Protein A/G. It would be great if you could share your comments, what to consider, advantages/disadvantages of Protein A/G immobilization for SPR.
I'm looking for a simple and quick way to immobilize Drosophila isolated CNS before Ca imaging without movement disturbance of the brain due to liquid containing stimuli application on it...
Any idea? tips?
I am working on research related to fabrication of glucose biosensor by using screen printed carbon electrodes (SPCE). I modified the working electrode with nanocomposite and then immobilised glucose oxidase-glutaraldehyde mixture on the modified SPCE.
Here are the detailed steps:
1. Preparation of nanocomposite.
2. Mix 20 μL of the 2% glutaraldehyde solution with 50 μL of Glucose oxidase. The mixture was allowed to sit for 30 minutes at room temperature before use.
3. Drop cast 3 μL of the nanocomposite onto the working electrode (WE) of SPCE.
Immobilization of Glucose oxidase-glutaraldehyde mixture:
1. Drop cast 3 μL of glucose oxidase-glutaraldehyde mixture on the modified SPCE
2. Allow the solution to adsorb onto the modified SPCE for 24 hours at room temperature.
3. After 24 hours, wash the unbound glucose oxidase from the working electrode using 0.01M PBS (pH 7).
4. Let the SPCE to dry at room temperature.
The MSDS mentioned that optimum storage temperature of glucose oxidase is -20°C.
As I am performing the immobilization of Glucose oxidase-glutaraldehyde mixture at room temperature for 24 hours, will it affect the stability of the glucose oxidase?
Plus, should I be storing the SPCE with immobilised glucose oxidase at room temperature or at cool temperature (probably 4°C)?
Help appreciated!! Thanks
I'm doing enzyme immobilization right now and I want to calculate the effectiveness factor, η based on this formula:
η =Vmax of immobilized enzyme/Vmax of free enzyme
Vmax to be put inside the formula above must come from one substrate concentration. But how to calculate Vmax from only one concentration of substrate? Because the usual way that I know, to calculate kinetic data including Km, Vmax, a varying substrate concentration is needed.
There's one paper I'm referring to and I don't know how they did that.
Is there any other way to calculate effectiveness factor?
Liquid carbon dots (CDs ) were synthesized with greenish color under UV-light. However, after mixing with PVA polymer, the color turned to blue with enhanced quantum yield (QY). what is the possible interaction made this enhancement? Is it related to hydrogen bonds of PVA or other reasons. Thanks in advance.
I wonder if it would be fine to try some test of encapsulation of oligonucleotides on or within the surface of porous silica gel (60) based TLC films, literature says it is posible to do, but, are there any protocol or directions to take into account?
The peptides have a very high specific signal to the target antibodies on the ELISA assay, but it did not work well on the NC membrane. The peptide was immobilized on the NC membrane with PBS buffer. I would like to ask any strategies which can improve the peptide affinity on the NC membrane assay. Is there any amino acid sequence that can be improved binding efficiency, spotting buffer and/or recommended size of peptide?
I'm trying to immobilize cellulase on Fe3O4 magnetic nanoparticles coated with Tannic acid, with glutaraldehyde as cross-linker. After the immobilization process, I washed nanoparticles four times and measured the protein amount of washing water with both Lowry and Bradford methods, with BSA as standard, but it is more than the protein amount of initial enzyme I added and the protein loading is negative. I calculated protein this way:
protein loading(%)= protein immobilized onto nanoparticles / amount of protein used*100
Enzyme immobilized onto nanoparticles (mg) = amount of protein used (mg) – the amount of protein in washing water (mg)
total protein of washing water (mg)= protein (mg/ml)* the volume of washing water (ml)
I know EDC has been proven to activate the carboxyl group on the substrate to attach amine-terminated particles.
In my work, I have carboxyl-terminated particles that I want to attach to the amine-terminated glass.
My question is Can I use the same protocol of the EDC?
The news in question is very revolutionary: Only an authority can help in such a case. Can a reader be so kind as to inform an authority if he or she happens to have the contact?
The news is that Zwicky was right in 1929 with his early explanation of the Hubble law. Cryodynamics, the now 9 years old sister discipline of the fundamental science of Thermodynamics, is the good news. But the world is too immobile to understand fast enough after its having failed to understand Zwicky for 3 generations.
The word needs to be spread that Einstein overlooked a fourth giant implication of his maverick "equivalence principle" of 1907. Fritz Zwicky first saw it and applied it correctly to cosmology in 1929. However, bad luck wills that the 91 years long IQ blunder of humankind -- of having failed to understand Zwicky 1929 -- entails geocidal consequencesas was first shown in a little paper in 2008.
Is there really no one able to heal a 91 years long dark age which now entails geocidal consequences ever since 2008?
Jan. 22, 2020
Recently I got a question which asked the minimum Nitrogen content for a Plant to check immobilization loss ???
Generally a Plant constitutes about 1.5-2% N in their body,which synthesized in their body in organic form.
Immobilization is a phenomena which implies Changing form of Inorganic to Organic & making one nutrient available form to unavailable form in Soil.
Then how is this possible for a Crop to control a phenomena which is occurring on soil by it's own N content ???