Properties of the multiple forms of the soluble 17α-hydroxy steroid dehydrogenase of rabbit liver
| Autor: | S Hasnain, D G Williamson |
|---|---|
| Rok vydání: | 1977 |
| Předmět: |
Stereochemistry
medicine.medical_treatment Biochemistry Steroid Estradiol Dehydrogenases chemistry.chemical_compound Glucosides Glucoside medicine Animals Glycosides Amino Acids Molecular Biology chemistry.chemical_classification Estradiol Molecular mass Epitestosterone Hydroxysteroid Dehydrogenases Substrate (chemistry) Cell Biology Glucuronic acid Molecular Weight Kinetics Enzyme Liver chemistry Glucuronide Research Article medicine.drug |
| Zdroj: | Biochemical Journal. 161:279-283 |
| ISSN: | 0264-6021 |
| DOI: | 10.1042/bj1610279 |
| Popis: | The six forms of the 17alpha-hydroxy steroid dehydrogenase purified from rabbit liver cytosol have very similar physical properties. The molecular weights of all the enzymes were within 3% of the average mol.wt of 39 600. Only one of the six enzymes showed a significant difference in amino acid composition. All but one form of the 17alpha-hydroxy steroid dehydrogenases exhibited greater activities towards the androgen, epitestosterone, than towards oestrogen substrates. With oestrogen substrates one enzyme displayed a high specificity towards the substrate oestradiol-17alpha 3-glucuronide. This high activity was lost if the glucuronic acid moiety was removed or replaced by glucose or galacturonic acid. The other enzyme forms had approximately equal activity toward oestradiol-17alpha and its glucuronide or glucoside derivative. However, substitution of galacturonic acid at C-3 of oestradiol-17alpha substantially decreased the activity of all but one enzyme form. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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