PROPERTIES AND TISSUE DISTRIBUTION OF MOUSE MONOMERIC CARBONYL REDUCTASE

We previously cloned a cDNA for mouse cerebellum carbonyl reductase wh ich shows more than 81% homology to the cDNAs for monomeric carbonyl r eductases of the rat, rabbit and human, and for pig 20 beta-hydroxyste roid dehydrogenase. In the present study, we expressed the recombinant monomeric enzyme (34 kDa and pI 8.3) from the cDNA and compared its p roperties with the recombinant human enzyme. The mouse and human enzym es showed similar functional properties, although they differed in kin etic constants for carbonyl substrates and in inhibitor sensitivity. B oth enzymes lacked glutathione S-transferase activity. Western blot an d reverse transcription-polymerase chain reaction analyses showed that the enzyme protein and its mRNA are expressed in various mouse tissue s.