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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 of similar structural determinants between the enzyme forms. Both have an apparent molecular mass of 32 kDa, suggesting protein modifications occurring in the type 1 isozyme which account for the differences in chromatographic behaviour.


Journal article



Publication Date





63 - 69


11-beta-Hydroxysteroid Dehydrogenase Type 1, Animals, Binding Sites, Chromatography, Affinity, Electrophoresis, Polyacrylamide Gel, Guinea Pigs, Hydroxysteroid Dehydrogenases, Immunoblotting, In Vitro Techniques, Isoenzymes, Liver, Microsomes, Liver, Molecular Weight, Subcellular Fractions, Substrate Specificity, Xenobiotics