Additional Possibility of Data Analysis of Enzyme Inhibition and Activation. 5. Comparative Study of Temperature Activation of Calf Alkaline Phosphatase and Escherichia coli Alkaline Phosphatase

It was shown that simultaneous account of a course of change in the maximum reaction rate (V) and the Michaelis constant (Km) by plotting their vector representations in the three-dimensional KmVt coordinate system allows additional analysis of the dynamics of enzyme temperature activation. It also makes it possible to study the mechanism of enzyme action under varying temperature conditions of technological processes by use of such new parameters of enzyme activation as: a) enzyme activation intensity, b) the overall enzyme activation effect, c) a geometrical portrait of enzyme activation. A comparative study of temperature activation of calf alkaline phosphatase and Escherichia coli alkaline phosphatase was performed by conventional and new methods of data processing.