PURIFICATION AND PARTIAL CHARACTERIZATION OF GLYOXALASE-I FROM A HIGHER-PLANT BRASSICA-JUNCEA

被引：27

作者：

DESWAL, R ^{[1
]}

SOPORY, SK ^{[1
]}

机构：

[1] JAWAHARLAL NEHRU UNIV,SCH LIFE SCI,PLANT RES LAB,NEW DELHI 110067,INDIA

来源：

FEBS LETTERS | 1991年 / 282卷 / 02期

关键词：

GLYOXALASE-I; ENZYME PURIFICATION; METHYLGLYOXAL; GLUTATHIONE; S-HEXYL GLUTATHIONE;

D O I：

10.1016/0014-5793(91)80494-N

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：

The glyoxalase I was purified from Brassica juncea by affinity chromatography on S-hexyl GSH sepharose 4B. Homogeneity of the protein was confirmed electrophoretically by a silver stained gel. Activity staining on a native starch gel also showed a single band. The effect of glutathione, methylglyoxal, and pH on enzyme kinetics was studied. Magnesium was found to stimulate the enzyme activity.

引用

页码：277 / 280

页数：4

共 20 条

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