PURIFICATION AND PROPERTIES OF SERINE HYDROXYMETHYLASE FROM SOLUBLE AND MITOCHONDRIAL FRACTIONS OF RABBIT LIVER

被引：59

作者：

FUJIOKA, M

机构：

[1] Department of Biochemistry, Osaka University School of Medicine, Osaka, College of Bio-Medical Technology, Toyonaka, Osaka

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1969年 / 185卷 / 02期

关键词：

D O I：

10.1016/0005-2744(69)90427-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Serine hydroxymethylase (l-serine tetrahydrofolate 5,10-hydroxymethyltransferase, EC 2.1.2.1) isoenzymes were purified separately from the soluble and mitochondrial fractions of rabbit liver. The purified preparations appeared to contain a single component in each case as judged from ultracentrifugation and eletrophoresis on polyacrylamide or starch gels. The isoenzymes had similar properties with respect to pH optimum, electrophoretic mobility as well as the reactions they catalyzed. The isoenzymes, however, were different immunochemically; the antiglobulin prepared against one of the isoenzymes did not inhibit the enzymic activity of the other. The molecular weights of the soluble fraction and the mitochondrial fraction enzymes, determined by the sedimentation equilibrium method, were approx. 185 000 and 170 000, respectively. Both isoenzymes contained 4 moles of pyridoxal phosphate per mole of enzyme. © 1969.

引用

页码：338 / &

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