A Second Thioltransferase of Schizosaccharomyces pombe Contains Glutathione S-transferase Activity

HONGGYUM KIM, Eun Hee Park, Chang Jin Lim

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14 Scopus citations

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 nitration, 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.

Original languageEnglish (US)
Pages (from-to)535-540
Number of pages6
JournalJournal of Biochemistry and Molecular Biology
Volume32
Issue number6
StatePublished - Nov 30 1999

Keywords

  • Glutaredoxin
  • Glutathione S-transferase
  • Schizosaccharomyces pombe
  • Thioltransferase

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