Jan 1, 1976

Kinetics of Ca 2+ or Mg 2+ activated ATPase from lymphocyte plasma membranes

Biochimie
B PauJ C Mani

Abstract

The kinetic study of the C2+ ATPase activity of lymphocyte plasma memebranes allowed some properties of this enzyme to be evidenced. The Ca2+-activated hydrolysis of ATP is independent of a non-specific alkaline phosphatase. The substrate of the ATPase activity is the chelate Ca2+- ATP. Mg2+ may substitute for Ca2+ both as chelating ion and as activating ion. Several results suggest that we have only one ATPase, activated either by Ca2+-, or by Mg2+ with less efficiency; both chelates hve the same Km; pH values for maximum activity and transition temperatures are identical; the effects of free ions are also the same, activation at low concentration and inhibition at high concentration.

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Mentioned in this Paper

Thermodynamics
Calcium
Lymphoid Cells
Alkaline Phosphatase
DNA-dependent ATPase
Hydrogen-Ion Concentration
Enzyme Activation
Plasma Membrane
Magnesium

About this Paper

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