p1. 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 iN/i-ethyl-maleimide, protection is afforded by 3-phosphoglycerate though not by NADsup+/sup./p
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