A second thioltransferase of Schizosaccharomyces pombe contains glutathione S-transferase activity
- Authors
- Kim, HG; Park, EH; Lim, CJ
- Issue Date
- 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
- Pages
- 6
- 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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