| Literature DB >> 4386930 |
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(+).Entities:
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Year: 1968 PMID: 4386930 PMCID: PMC1187024 DOI: 10.1042/bj1090743
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857