Thursday, 23 July 2015

What is vmax and km in enzyme kinetics

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Aloe: MedlinePlus Supplements


  http://www.nlm.nih.gov/medlineplus/druginfo/natural/607.html
Early research suggests that applying a cream containing aloe to the skin for 2 weeks increases the amount of water in the outermost later of the skin, but not on the inner layers. Some preliminary evidence suggests that applying aloe gel does not improve the healing rate of bedsores compared to management with gauze moistened with salt water

Madarosis: A Marker of Many Maladies


  http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3358936/
Hair growth usually starts by 12 weeks, and it reaches its peak by about 12 months.Topic prostaglandin analogues are used for the treatment of glaucoma. The development of the eyelashes is apparent initially as proliferation of the surface epithelial cells into the underlying mesenchyme while maintaining an intact basal lamina

  http://www.public.asu.edu/~laserweb/woodbury/classes/chm467/Enzkin/alkphosphat.html
Any increase in absorbance values obtained from this sample should be subtracted from the corresponding time readings in your enzyme catalyzed reactions before constructing final plots

13B: Chemical Kinetics - Chemwiki


  http://chemwiki.ucdavis.edu/Analytical_Chemistry/Analytical_Chemistry_2.0/13_Kinetic_Methods/13B%3A_Chemical_Kinetics
Example 13.7 Practice Exercise 13.3 provides kinetic data for the oxidation of catechol (the substrate) to o-quinone by the enzyme o-diphenyl oxidase in the absence of an inhibitor. One advantage of a chemical kinetic method is that we often can adjust the reaction conditions so that the analyte and the interferent have different reaction rates

Substrate Concentration (Introduction to Enzymes)


  http://www.worthington-biochem.com/introbiochem/substrateconc.html
Substrate Concentration It has been shown experimentally that if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will increase until it reaches a maximum. Using this maximum velocity and equation (7), Michaelis developed a set of mathematical expressions to calculate enzyme activity in terms of reaction speed from measurable laboratory data

Diabetic cardiac autonomic neuropathy, inflammation and cardiovascular disease


  http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3580884/
Established risk factors for CAN are glycemic control in type 1 diabetes, and a combination of hypertension, dyslipidemia, obesity and glycemic control in type 2 diabetes25. There is an association between CAN and more severe intraoperative hypothermia43 that can result in decreased drug metabolism and impaired wound healing

  http://www.naturalfactors.com/caen/products/detail/2877/papaya-enzymes
Because they are efficient at breaking down protein, carbohydrates, and fats, they stimulate the good bacteria in the digestive tract, detoxify and cleanse the colon

  http://dwb4.unl.edu/Chem/CHEM869K/CHEM869KLinks/www.curvefit.com/introduction63.htm
To fit these kind of data (called an enzyme progress curve) you need to use a program that can fit data to a model defined by differential equations or by an implicit equation. If the initial transient phase is very short, you can simply measure product formed at a single time, and define the velocity to be the concentration divided by the time interval

  http://dwb4.unl.edu/Chem/CHEM869K/CHEM869KLinks/jeffline.tju.edu/CWIS/DEPT/biochemistry/kinetics/HTML/PAGE8.HTML
The views or opinions expressed in the resources provided do not necessarily reflect those of Thomas Jefferson University, Thomas Jefferson University Hospital, or the Jefferson Health System or staff

Enzyme kinetics laboratory report


  http://www.ukessays.com/essays/chemistry/enzyme-kinetics-laboratory-report.php
Finally KM is an approximate measure of the affinity of an enzyme for its substrate.A small value of KM indicates a high affinity of the enzyme for the substrate. Its primary mechanism of action is to bring a substrate molecule into contact with a molecule of water .This results in catalysis and the removal of phosphate group

Enzyme Kinetics Lab - The Relationship Between Enzyme and Substrate Concentrations and Rates of Reaction


  http://adamcap.com/schoolwork/enzyme-kinetics-lab-the-relationship-between-enzyme-and-substrate-concentrations-and-rates-of-reaction/
A reaction mixture consisting of 0.850 ml distilled water, 1.000 ml buffer stock, 0.100 ml 15 mM NAD+, and 1.000 ml ethanol was then put into the test tube using a micropipettor. Discussion Shono and co-workers (1995) observed the rate of reaction versus the concentration of a substrate different from the one used in this experiment

Kinetics of Catalase and Dehydrogenase in Main Soils of Northeast China under Different Soil Moisture Conditions


  http://www.medwelljournals.com/fulltext/?doi=aj.2009.113.120
Maybe slightly and intensely changed Km values of dehydrognease and catalase are attributed to different origins of microorganisms and different existing sites in the microorganisms. Catalase and dehydrogenase are intracellular enzymes that are involved in microbial oxidoreductase metabolism and the kinetic parameters (Vmax and Km) are important to establish the efficiency of catalysis by the intracellular enzymes

  http://bcrc.bio.umass.edu/intro/content/enzyme-kinetics-lab-protocol
We have a range of monosaccharides and disaccharides (glucose, lactose, galactose and sucrose) that can be tested to see if they inhibit the ability of Lactase to convert ONPG to o-nitrophenol (ONP). You will have the following materials available: Enzyme: Lactase Substrate: ONPG, various concentrations provided Potential inhibitors: Sucrose, Lactose, Galactose, Glucose NOTE: in order to add the inhibitor to the reaction you should decrease the amount of media in the reaction to make up for what you are adding for inhibitors

Effect of Substrate Concentration on Enzyme Kinetics (Theory) : Biochemistry Virtual Lab II : Biotechnology and Biomedical Engineering : Amrita Vishwa Vidyapeetham Virtual Lab


  http://vlab.amrita.edu/?sub=3&brch=64&sim=1090&cnt=1
at low substrate concentration the active sites on molecules (enzyme) are not occupied by substrate and the enzyme rate varies with substrate molecules concentration (phase1). In the study of substrate concentration on enzyme kinetics, the enzyme is kept constant where as the concentration of Starch is taken in increasing order

  http://forums.studentdoctor.net/threads/km-and-vmax.653761/
The reason Km increases with a competitive inhibitor is because the inhibitor is directly competing with the substrate for a fixed number of active sites on enzymes. but how can you tell if something is a strong base or weak acid? Also, during a titration with an amino acid, such as alanine, with a strong base, the COOH is depronated first, which leaves it with a negative charge, and it is still acidic (low pH), but I thought that a positive charge on the Nitrogen is what made it acidic

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