Rat Ovarian 20±-Hydroxysteroid Dehydrogenase-1 May Belong to Aldo-Keto Reductase Superfamily

Ken Noda, Kunio Shiota, Tomoya Ogawa, Shintaro Yagi, Michio Takahashi

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


We have previously purified the 20±hydroxysteroid dehydrogenase (20±HSD) molecule from normal mature rat ovarian cytosol [Biochim. Biophys. Acta, 1991, 1079: 112-118]. In order to further characterize the 20±HSD and to obtain information for molecular cloning of the enzyme, we determined its N-terminal amino acid sequence. The sequence was shown to be Ser-Lys-lle-Gln-Lys-Met-Glu-Leu-Asn-Asp-Gly-His-Ser-lle-Pro-Val-Leu-Gly-Phe-Xaa-Thr. A search of the SWISS-PROT protein sequence database for N-terminal amino acid sequence similarities revealed 6 highly homologous proteins, including bovine prostaglandin F synthase, rat liver 3±hydroxysteroid dehydrogenase, bovine lens aldose reductase, human aldose reductase, frog 3±crystallin and human liver chlordecone reductase, suggesting that rat ovarian 20ar-HSD belongs to the aldo-keto reductase gene superfamily.

Original languageEnglish
Pages (from-to)169-173
Number of pages5
JournalJournal of Reproduction and Development
Issue number2
Publication statusPublished - 1993
Externally publishedYes


  • 20α-Hydroxy steroid dehydrogenase
  • Aldo-keto reductase
  • Automatic Edman degradation
  • N-terminal amino acid sequence

ASJC Scopus subject areas

  • Animal Science and Zoology


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