Jan 1, 1975

Further characterization of the association of glyceraldehyde-3-phosphate dehydrogenase with reticulocyte membranes

Acta biologica et medica Germanica
G Letko, R Bohnensack

Abstract

1. The behaviour and properties of membrane-bound GAPDH of rabbit reticulocytes were investigated. 2. The bound GAPDH is more resistant to inactivation by KCl than the soluble enzyme (allotopy). 3. The bound enzyme is released by electrolytes. This effect does not only depend on the ionic strength but additionally on the kind of ions, pH-value and protein concentration. 4. A comparison of the releasing effect of NAD analogues shows the necessity of the 5'-AMP moiety in the structure of the effector. 5. The represented results demonstrate the specifity of the GAPDH-membrane binding in rabbit reticulocytes.

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Mentioned in this Paper

Reticulocytes
Blood
Glyceraldehyde-3-Phosphate Dehydrogenases
Hemolysis
Hydrogen-Ion Concentration
Plasma Membrane
GAPDH

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