V. I. Krupyanko
G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142290 Pushchino, Prospect Nauki 5, Moscow region, Russia
P. V. Krupyanko
G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142290 Pushchino, Prospect Nauki 5, Moscow region, Russia
ABSTRACT
Possible use of the criterion of stability of the mechanism of proceeding of enzymatic reactions for studying the effect of increasing concentration of inhibitors on the enzyme were analysed. It was shown that the constant of inhibition (Ki) characterizes the strength of binding of the inhibitor to the enzyme. The length of Li vectors for enzyme inhibition in three-dimensional K` mV` I coordinate system characterizes the intensity of inhibition. This opens up additional possibility of studying the mechanism of proceeding of enzymatic reactions at consecutive addition of inhibitors, activators and also under varying temperature conditions, etc., with the aim to increase the yield of a reaction product. Examples of using the dependencies of change in the length of Li vectors of enzyme inhibition for characterization of the dynamics of a stable and unstable inhibitory effect on calf alkaline phosphatase are given.
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How to cite this article
V. I. Krupyanko and P. V. Krupyanko, 2005. Additional Possibility of Data Analysis of Enzyme Inhibition and Activation. 4. Criterion of Stability of the Mechanism of Proceeding of Enzymatic Reactions. Journal of Biological Sciences, 5: 292-296.
DOI: 10.3923/jbs.2005.292.296
URL: https://scialert.net/abstract/?doi=jbs.2005.292.296
DOI: 10.3923/jbs.2005.292.296
URL: https://scialert.net/abstract/?doi=jbs.2005.292.296