Nov 26, 1975

Purification of human red cell glucose 6-phosphate dehydrogenase by affinity chromatography

Journal of Chromatography
A Yoshida

Abstract

Human glucose 6-phosphate dehydrogenase associated with NADPH was efficiently bound with agarose-bound NADP, whereas the enzyme associated with NADP was poorly bound with agarose-bound NADP. After the elimination of haemoglobin from haemolyzate by treatment with DEAE-cellulose, the enzyme was converted into the NADPH-bound form and was applied on an affinity column. The enzyme was specifically eluted from the column by NADP in the elution buffer. A homogeneous enzyme preparation was obtained in high yield.

Mentioned in this Paper

Buffers
G6PD
Chromatography, DEAE-Cellulose
Phosphate Measurement
Glucosephosphate Dehydrogenase
Ampholytes
Enzyme agent
DEAE-Cellulose
Hemoglobin Measurement
Purification Aspects

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