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The Effect of Temperature and pH on Enzyme Activity

  • Chapter
Initial Rate Enzyme Kinetics

Part of the book series: Molecular Biology Biochemistry and Biophysics ((MOLECULAR,volume 22))

Abstract

It has long been recognized that enzyme catalysis is markedly influenced by alterations in the hydrogen ion concentration. MICHAELIS and DAVIDSOHN (1) in 1911 attempted to explain the characteristic bell-shaped velocity versus pH curve obtained for many enzyme catalyzed reactions. They proposed that the enzyme, which was assumed to be amphoteric, could exist in its acidic, basic or isoelectric form, and they suggested that it was this latter state of the enzyme that was catalytically active. Subsequent experimental studies of pH kinetics led MICHAELIS and ROTHSTEIN to propose in 1920 (2) that it was the ionization state of the enzyme substrate complex, rather than of the free enzyme, that caused changes in the rate of catalysis as pH is altered. However, it remained for HALDANE some ten years later to suggest that it was the charge distribution associated with certain functional groups on the enzyme, rather than the isoelectric point of the enzyme, that was responsible for the observed alterations in the rates of enzyme catalysis induced by changes in hydrogen ion concentration (3).

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Authors and Affiliations

  1. Biochemistry and Biophysics Department, Iowa State University, Ames, IA, 50010, USA

    Professor Herbert J. Fromm Ph. D.

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  1. Professor Herbert J. Fromm Ph. D.
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© 1975 Springer-Verlag Berlin Heidelberg

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Fromm, H.J. (1975). The Effect of Temperature and pH on Enzyme Activity. In: Initial Rate Enzyme Kinetics. Molecular Biology Biochemistry and Biophysics, vol 22. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80966-8_8

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  • DOI: https://doi.org/10.1007/978-3-642-80966-8_8

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-80968-2

  • Online ISBN: 978-3-642-80966-8

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