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

Authors
Kim, HGPark, EHLim, CJ
Issue Date
30-Nov-1999
Publisher
SPRINGER SINGAPORE PTE LTD
Keywords
glutaredoxin; glutathione S-transferase; Schizosaccharomyces pombe; thioltransferase
Citation
JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.32, no.6, pp.535 - 540
Journal Title
JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY
Volume
32
Number
6
Start Page
535
End Page
540
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/16814
ISSN
1225-8687
Abstract
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.
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