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KMID : 0380219990320060535
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Journal of Biochemistry and Molecular Biology
1999 Volume.32 No. 6 p.535 ~ p.540
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A Second Thioltransferase of Schizosaccharomyces pombe Contains Glutathione S-transferase Activity
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Kim Hong-Gyum
Park Eun-Hee
Lim Chang-Jin
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Abstract
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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 (14kDa) 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.
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KEYWORD
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Glutaredoxin, Glutathione S-transferase, Schizosaccharomyces pombe, Thioltransferase
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