Functional and immunological relationships between metyrapone reductase from mouse liver microsomes and 3 alpha-hydroxysteroid dehydrogenase from Pseudomonas testosteroni.

Journal article

3 Alpha-hydroxysteroid dehydrogenase (3 alpha-HSD) from Pseudomonas testosteroni was shown to reduce the xenobiotic carbonyl compound metyrapone (MPON). Reversely, MPON reductase purified from mouse liver microsomes and previously characterized as aldehyde reductase, was competitively inhibited by 3 alpha-HSD steroid substrates. For MPON reduction both enzymes can use either NADH or NADPH as co-substrate. Immunoblot analysis after native and SDS gel electrophoresis of 3 alpha-HSD gave a speci...

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Authors: Maser, E; Oppermann, U; Bannenberg, G; Netter, K

• Journal: FEBS letters
• Volume: 297
• Issue: 1-2
• Pages: 196-200
• Publication date: 1992-02-01
• DOI: 10.1016/0014-5793(92)80359-o
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: Alcohol Oxidoreductases; Hydroxysteroid Dehydrogenases; Mice; Substrate Specificity; Pseudomonas; Animals; Cross Reactions; Female; Oxidation-Reduction; Blotting, Western; Microsomes, Liver; NADP; Electrophoresis, Polyacrylamide Gel; NAD