PURIFICATION AND STUDY OF A BACTERIAL GLUTATHIONE S-TRANSFERASE

被引：36

作者：

ARCA, P ^{[1
]}

GARCIA, P ^{[1
]}

HARDISSON, C ^{[1
]}

SUAREZ, JE ^{[1
]}

机构：

[1] UNIV OVIEDO,FAC MED,AREA MICROBIOL,JULIAN CLAVERIA SN,E-33006 OVIEDO,SPAIN

来源：

FEBS LETTERS | 1990年 / 263卷 / 01期

关键词：

(Escherichia coli); Enzyme purification; Glutathione transferase; N-terminal sequence; Western blotting;

D O I：

10.1016/0014-5793(90)80709-R

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：

A glutathione S-transferase from Escherichia coli has been purified approximately 800-fold with an 11% activity yield by passage through DEAE Sephacel and glutathione-agarose affinity columns. Its functional form is a homodimer of two 24 000 Da polypeptides that catalyzes the binding of glutathione and 1-chloro-2,4-dinitrobenzene withKm values of 0.25 and 1.5 mM, respectively. Optima of pH and temperature were 7.5 and 35°C. The activity was stimulated (30%) by ethylenediaminetetraacetic add. The N-tenninal amino acid sequence was: Met-Leu-Leu-Phe-Ile-Leu-Pro-Gly-Ala. © 1990.

引用

页码：77 / 79

页数：3

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