Abstract
11β-hydroxysteroid dehydrogenase (11β-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 11β-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 11β-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.
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