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. 1968 Oct;109(5):743-8.
doi: 10.1042/bj1090743.

The isolation and characterization of 3-phosphoglycerate dehydrogenase from peas

J C Slaughter, D D Davies

The isolation and characterization of 3-phosphoglycerate dehydrogenase from peas

J C Slaughter et al. Biochem J. 1968 Oct.

Abstract

1. 3-Phosphoglycerate dehydrogenase was purified 400-fold from crude extracts of etiolated pea epicotyls. 2. Michaelis constants were determined for all four substrates. 3. Loss of sensitivity to inhibition by l-serine occurs on purification. 4. The purified enzyme is inhibited by thiol-group reagents and, with N-ethyl-maleimide, protection is afforded by 3-phosphoglycerate though not by NAD(+).

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