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Platelet AMP deaminase. Purification and kinetic studies.

Authors
  • Ashby, B
  • Holmsen, H
Type
Published Article
Journal
The Journal of biological chemistry
Publication Date
Oct 25, 1981
Volume
256
Issue
20
Pages
10519–10523
Identifiers
PMID: 7287721
Source
Medline
License
Unknown

Abstract

AMP deaminase has been purified to homogeneity from human platelets by phosphocellulose chromatography. Kinetic studies showed sigmoidal behavior as a function of AMP concentration with the midpoint of the saturation curve (S0.5) at 3.5 and 4.0 mM in NaCl and KCl, respectively, at pH 6.5. Activation by saturating ATP converted the velocity versus substrate plot to hyperbolic with a Michaelis constant of 1.2 mM and the same maximum velocity in either salt. Addition of increasing concentrations of GTP in the presence of NaCl led to activation followed by inhibition whereas GTP in the presence of KCl gave inhibition with no apparent activation.

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