Thioltransferase from Schizosaccharomyces pombe: Purification to homogeneity and some properties

Hong Gyum Kim, Eun Hee Park, Chang Jin Lim

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11 Scopus citations


Two types of thioltransferase were identified in the cytosolic extract of Schizosaccharomyces pombe, a fission yeast. In the present study, the major one of them was purified to homogeneity using chromatography processes such as ion-exchange chromatography and gel filtration. Purification was monitored by the transhydrogenase activity of thioltransferase with 2-hydroxyethyl disulfide as a substrate. Its molecular weight was estimated to be about 14,000 on SDS-polyacrylamide gel electrophoresis. The purified enzyme catalyzes the reduction of various disulfide compounds such as S-sulfocysteine, L-cystine, and insulin. It was also found to contain the reducing activity on non-disulfide substrates such as dehydroascorbic acid and alloxan. Its activity was greatly activated by high concentrations of reduced glutathione. It was found to be very heat-stable as like other thioltransferases. It was characterized on other aspects such as kinetic parameters and optimal reaction conditions.

Original languageEnglish (US)
Pages (from-to)431-437
Number of pages7
JournalMolecules and cells
Issue number4
StatePublished - Aug 31 1998


  • Glutaredoxin
  • Schizosaccharomyces pombe
  • Thioltransferase


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