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

Acta biologica et medica Germanica

Jan 1, 1975

G Letko, R Bohnensack

PMID: 880

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 ion...read more

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Hydrogen-Ion Concentration
Reticulocytes
Blood
Plasma Membrane
GAPDH
Glyceraldehyde-3-Phosphate Dehydrogenases
Hemolysis
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Further characterization of the association of glyceraldehyde-3-phosphate dehydrogenase with reticulocyte membranes

Acta biologica et medica Germanica

Jan 1, 1975

G Letko, R Bohnensack

PMID: 880

DOI:

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 ion...read more

Mentioned in this Paper

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

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