Properties and tissue distribution of mouse monomeric carbonyl reductase

Shuhei Ishikura, Yutaka Yamamoto, Kazuya Matsuura, Jianjun Wei, M. E. Hodes, Akira Hara*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


We previously cloned a cDNA for mouse cerebellum carbonyl reductase which shows more than 81% homology to the cDNAs for monomeric carbonyl reductases of the rat, rabbit and human, and for pig 20β-hydroxysteroid dehydrogenase. In the present study, we expressed the recombinant monomeric enzyme (34 kDa and pI 8.3) from the cDNA and compared its properties with the recombinant human enzyme. The mouse and human enzymes showed similar functional properties, although they differed in kinetic constants for carbonyl substrates and in inhibitor sensitivity. Both enzymes lacked glutathione S-transferase activity. Western blot and reverse transcription- polymerase chain reaction analyses showed that the enzyme protein and its mRNA are expressed in various mouse tissues.

Original languageEnglish (US)
Pages (from-to)879-881
Number of pages3
JournalBiological and Pharmaceutical Bulletin
Issue number8
StatePublished - 1998


  • Carbonyl reductase
  • Short-chain dehydrogenase/reductase family
  • Tissue distribution
  • mRNA expression

ASJC Scopus subject areas

  • Pharmacology
  • Pharmaceutical Science


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