When calculating enzyme energy activation (Eα), researchers tend to only plot a temperature dependence of the course of change in the logarithm (lg V) of maximum reaction rate upon (1/T�K) and determine these thermodynamic parameters by the slope angle (tg α) of experimental lines in the (lg V;1/T) coordinates of Arrhenius. Yet, the course of change in the Michaelis constant (Km), the second important parameter of enzyme activation, is not taken into consideration as there is no this parameter in the Arrhenius equation. In practice, simultaneous account of temperature dependence in the course of change of both V and Km parameters allows additional analysis of the dynamics of enzyme temperature activation. A vector method of representation of such data in the three-dimensional KmVt coordinate system is proposed. Examples of data processing in temperature activation of bovine pyrimidine-specific RNases A and B using conventional methods and the proposed one are given.
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P.V. Krupyanko, V.I. Krupyanko and I.N. Dorokhov, 2005. Additional Possibility of Data Analysis of Enzyme Inhibition and Activation 3. Geometrical Portraits of Enzymatic Reactions for Data Processing in Enzyme Temperature Activation. Journal of Biological Sciences, 5: 98-102.
- 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.