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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.

Original publication

DOI

10.1016/s0300-483x(99)00191-2

Type

Journal article

Journal

Toxicology

Publication Date

04/2000

Volume

144

Pages

63 - 69

Addresses

Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S 171 77, Stockholm, Sweden. udo.oppermann@mbb.ki.se

Keywords

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