The isolation of serine transhydroxymethylase from bovine brain.
作者： Dillard S. Broderick , Kathleen L. Candland , James A. North , John H. Mangum
DOI: 10.1016/0003-9861(72)90131-2
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摘要: Abstract Serine transhydroxymethylase has been purified 150-fold from bovine brain. The initial fractionation with portamine sulfate and ammonium was followed by chromatography on DEAE-Cellulose Sephadex G-200. cofactor requirements for brain serine included pyridoxal phosphate tetrahydrofolate. maximum catalytic activity occurred at pH 7.6 the Michaelis constant 6.7 × 10 −4 m .
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