Heterogeneity of 11beta-hydroxysteroid dehydrogenase type 1/microsomal carbonyl reductase (11beta-HSD/CR) in guinea pig tissues. Purification of the liver form suggests modification in the cosubstrate binding site.

Journal article

11beta-hydroxysteroid dehydrogenase (11beta-HSD) and xenobiotic carbonyl reductase activities were determined in guinea pig tissue microsomes. The data indicate the presence of a NADP(H) dependent form, distinct from the known type I isozyme. Purification of 11beta-HSD-1 from liver microsomes resulted in two distinct peaks, resolved by dye-ligand chromatography, indicating differences in the cosubstrate binding site. Immunoblot analysis using anti 11beta-HSD-1 antibodies reveals the presence ...

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Authors: Oppermann, U; Möbus, E; Nagel, G; Maser, E

• Journal: Toxicology
• Volume: 144
• Issue: 1-3
• Pages: 63-69
• Publication date: 2000-04-01
• DOI: 10.1016/s0300-483x(99)00191-2
• EISSN: 1879-3185
• ISSN: 0300-483X
• Language: English
• Keywords: Binding Sites; Electrophoresis, Polyacrylamide Gel; Animals; Xenobiotics; Liver; Guinea Pigs; Immunoblotting; 11-beta-Hydroxysteroid Dehydrogenase Type 1; Substrate Specificity; Microsomes, Liver; Subcellular Fractions; Molecular Weight; Chromatography, Affinity; Hydroxysteroid Dehydrogenases; Isoenzymes