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The Effect of Temperature and pH on Enzyme Activity

  • Herbert J. Fromm
Part of the Molecular Biology Biochemistry and Biophysics book series (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).

Keywords

Free Enzyme Enzyme Catalysis Activation Entropy Proton Binding Maximal Initial Velocity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1975

Authors and Affiliations

  • Herbert J. Fromm
    • 1
  1. 1.Biochemistry and Biophysics DepartmentIowa State UniversityAmesUSA

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