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  • Title: Purification and characterization of carbonyl reductases from bovine liver cytosol and microsome. The cytosolic enzyme has a novel 3 alpha/17 beta-hydroxysteroid dehydrogenase activity.
    Author: Terada T, Niwase N, Koyama I, Imamura M, Shinagawa K, Toya H, Mizoguchi T.
    Journal: Int J Biochem; 1993 Sep; 25(9):1233-9. PubMed ID: 8224367.
    Abstract:
    1. Carbonyl reductase, which is distributed in both cytosolic and microsomal fractions in bovine liver, were purified to homogeneity on 12.5% sodium dodecylsulfate-polyacrylamide gel electrophoresis and shown to have molecular weights of 32 kDa and 68 kDa, respectively. 2. Both carbonyl reductases can catalyze the reduction of many carbonyl compounds including ketone, quinones and aldehyde with relatively low Km values. 3. From the absorption spectrum result, microsomal carbonyl reductase closely resembles cytochrome P-450 reductase. 4. Cytosolic carbonyl reductase is a novel enzyme which can act on both testosterone and androsterone at low concentration.
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