A second thioltransferase of Schizosaccharomyces pombe contains glutathione S-transferase activity

被引：0

作者：

Kim, HG

Park, EH

Lim, CJ ^{[1
]}

机构：

[1] Kangwon Natl Univ, Dept Life Sci, Chunchon 200701, South Korea

[2] Sookmyung Womens Univ, Coll Pharm, Seoul 140742, South Korea

来源：

JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY | 1999年 / 32卷 / 06期

关键词：

glutaredoxin; glutathione S-transferase; Schizosaccharomyces pombe; thioltransferase;

D O I：

暂无

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：

Two types of the thioltransferase (also called glutaredoxin) have been previously detected in the cytosolic extract of Schizosaccharomyces pombe, a fission yeast. Previously, the one with a smaller molecular mass (14 kDa) was purified and characterized. In the present study, the second thioltransferase was purified. The purification procedure included ammonium sulfate fractionation (40-80%), Sephadex G-200 gel filtration, DEAE-cellulose ion-exchange chromatography, Sephadex G-50 gel filtration, and glutathione-agarose affinity chromatography. The purified enzyme showed a single band on SDS-PAGE, and its molecular mass was determined to be 23 kDa, It utilizes various compounds as substrates, including 2-hydroxyethyl disulfide. Interestingly, we found that the purified thioltransferase also contains significant glutathione S-transferase activity.

引用

页码：535 / 540

页数：6

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