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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, Ralf Bohnensack

PMID: 880

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

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

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