The isolation and characterization of 3-phosphoglycerate dehydrogenase from peas
- 1 October 1968
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 109 (5) , 743-748
- https://doi.org/10.1042/bj1090743
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+.Keywords
This publication has 11 references indexed in Scilit:
- Inhibition of 3-phosphoglycerate dehydrogenase by l-serineBiochemical Journal, 1968
- Nicotinamide–adenine dinucleotide-specific isocitrate dehydrogenase from pea mitochondriaBiochemical Journal, 1967
- Synthesis of serine in the liver of vertebratesComparative Biochemistry and Physiology, 1966
- Comparative Studies on the Pathways for Serine Biosynthesis in Animal TissuesJournal of Biological Chemistry, 1966
- The Biosynthesis of Serine in Mouse Brain ExtractsJournal of Biological Chemistry, 1965
- Purification and Properties of Chicken Liver D-3-Phosphoglycerate Dehydrogenase*Biochemistry, 1965
- The Pathway and Control of Serine Biosynthesis in Escherichia coliJournal of Biological Chemistry, 1963
- Chromatography of some 2,4-dinitrophenylhydrazones in acid systemsJournal of Chromatography A, 1962
- THE STEREOSPECIFICITY OF ENZYMATIC HYDROGEN TRANSFER FROM DIPHOSPHOPYRIDINE NUCLEOTIDEJournal of Biological Chemistry, 1957
- THE ENZYMATIC REDUCTION OF HYDROXYPYRUVIC ACID TO d-GLYCERIC ACID IN HIGHER PLANTSJournal of Biological Chemistry, 1954