PURIFICATION AND PROPERTIES OF ARGINASE FROM SOYBEAN, GLYCINE-MAX, AXES

被引：51

作者：

KANG, JH ^{[1
]}

CHO, YD ^{[1
]}

机构：

[1] YONSEI UNIV,COLL SCI,DEPT BIOCHEM,SEOUL 120749,SOUTH KOREA

来源：

PLANT PHYSIOLOGY | 1990年 / 93卷 / 03期

关键词：

D O I：

10.1104/pp.93.3.1230

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Arginase (EC 3.5.3.1) was purified to homogeneity from cytosol of soybean, Glycine max, axes by chromatographic separations on Sephadex G-200, DEAE-sephacel, hydroxyapatite, and arginine-affinity columns. The molecular weight of the enzyme estimated by pore gradient gel electrophoresis was 240,000, while sodium dodecyl sulfate polyacrylamide gel electrophoresis gave a single band at the molecular weight of 60,000. The optimal pH for activity was 9.5 and the Km value was 83 millimolar. The enzyme was stimulated by polyamines such as putrescine.

引用

页码：1230 / 1234

页数：5

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