Membrane-bound Inorganic Pyrophosphatase of Human Erythrocytes.

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Purification and some properties of inorganic pyrophosphatase from human erythrocytes.

Inorganic pyrophosphatase was purified BOO-fold from human erythrocytes by a procedure involving complete hemolysis of the cells, removal of hemoglobin, ammonium sulfate fractionation, diethylaminoethyl cellulose column chromatography, and gel filtration. Magnesium chloride and 2-mercaptoethanol stabilized the activity. The procedure yielded an enzyme with an optimal pH of 7.7, and an apparent ...

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ژورنال

عنوان ژورنال: Acta Chemica Scandinavica

سال: 1971

ISSN: 0904-213X

DOI: 10.3891/acta.chem.scand.25-1457