ABSTRACT
By studying the inhibitory effect of increasing concentration of sodium tungstate on calf and porcine alkaline phosphatase and that of sodium molybdate on calf alkaline phosphatase, the perspectiveness of using the geometrical portraits of enzymatic reactions was shown for analysis of the mechanism of proceeding of biotechnological, pilot-plant and laboratory processes catalyzed by enzymes under varying conditions, such as, increasing concentration of inhibitors, activators and other introduced reaction components; change in ionic strength of the medium; temperature increase etc. The new method permits to provide higher yield of the reaction product and select the enzyme most stable to the particular conditions of a certain process.
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V.I. Krupyanko, P.V. Krupyanko and I.N. Dorokhov, 2005. Additional Possibility of Data Analysis of Enzyme Inhibition and Activation 2. Geometrical Portraits of Enzymatic Reactions for Data Processing in Enzyme Inhibition. Journal of Biological Sciences, 5: 92-97.
DOI: 10.3923/jbs.2005.92.97
URL: https://scialert.net/abstract/?doi=jbs.2005.92.97
DOI: 10.3923/jbs.2005.92.97
URL: https://scialert.net/abstract/?doi=jbs.2005.92.97
REFERENCES
- Krupyanko, V.I. and P.V. Krupyanko, 1999. Selection of substrate concentrations for determining the Michaelis constant and maximum rate of an enzymatic reaction. Applied Biochem. Microbiol., 35: 116-119.
Direct Link - Krupyanko, V.I., 2005. Additional possibility of data analysis of enzyme inhibition and activation.1: Equations for calculation of the ka and ki constants of enzyme activation and nontrivial types of enzyme inhibition. J. Biol. Sci., 5: 82-95.
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