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- W2045576475 abstract "1. The purity of rat liver cystathionine synthetase-serine deaminase was more than doubled over that previously reported through the use of zone electrophoresis. The ratio of the two enzymic activities of the more purified preparation remained unchanged. 2. Enzymic activity was slightly inhibited by certain pyridoxine derivatives and strongly inhibited by carbonyl reagents, sulfhydryl reagents, various metal chelating agents, and by a number of heavy metal ions. Mg++ and Mn++ slightly stimulated the serine deaminase activity. 3. Study of the substrates specificity of the enzyme showed that only L-serine and L-threonine were deaminated and only homocysteine was utilized for synthesis of a sulfur-containing diamino acid with L-serine. L-cysteine strongly inhibited cystathionine" @default.
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- W2045576475 date "1960-01-01" @default.
- W2045576475 modified "2023-10-14" @default.
- W2045576475 title "Further studies on cystathionine synthetase-serine deaminase of rat liver" @default.
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- W2045576475 doi "https://doi.org/10.1016/0006-3002(60)90783-6" @default.
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