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.
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 result...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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2000
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| _version_ | 1797094386480185344 |
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| author | Oppermann, U Möbus, E Nagel, G Maser, E |
| author_facet | Oppermann, U Möbus, E Nagel, G Maser, E |
| author_sort | Oppermann, U |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T04:13:25Z |
| format | Journal article |
| id | oxford-uuid:c8952eb4-9e23-4f15-be89-81e709929aa1 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T04:13:25Z |
| publishDate | 2000 |
| record_format | dspace |
| spelling | oxford-uuid:c8952eb4-9e23-4f15-be89-81e709929aa12022-03-27T06:53:13ZHeterogeneity 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 articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:c8952eb4-9e23-4f15-be89-81e709929aa1EnglishSymplectic Elements at Oxford2000Oppermann, UMöbus, ENagel, GMaser, E11beta-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. |
| spellingShingle | Oppermann, U Möbus, E Nagel, G Maser, E 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. |
| title | 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. |
| title_full | 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. |
| title_fullStr | 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. |
| title_full_unstemmed | 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. |
| title_short | 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. |
| title_sort | 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 |
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