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Journal of Biological Sciences

Year: 2005 | Volume: 5 | Issue: 4 | Page No.: 430-435
DOI: 10.3923/jbs.2005.430.435
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
V. I. Krupyanko, P. V. Krupyanko and V. V. Belozerov

Abstract: 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.

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How to cite this article
V. I. Krupyanko, P. V. Krupyanko and V. V. Belozerov, 2005. 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. Journal of Biological Sciences, 5: 430-435.

Keywords: Alkaline phosphatases, activation energy, intensity activation and geometrical portrait of enzyme activation

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