METHYLATION OF ESTRADIOL-17β BY A PARTIALLY PURIFIED PREPARATION OF BOVINE PINEAL HYDROXY-INDOLE-O-METHYLTRANSFERASE1
| Autor: | Judith Weisz, Tom Lloyd, Laura V. O’Brien |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
chemistry.chemical_classification
Indole test medicine.medical_specialty Methyltransferase Chromatography Kinetics Methylation Thin-layer chromatography law.invention Endocrinology Enzyme chemistry law Internal medicine medicine Crystallization hormones hormone substitutes and hormone antagonists Melatonin biosynthetic process |
| Zdroj: | Endocrinology. 102:330-333 |
| ISSN: | 1945-7170 0013-7227 |
| DOI: | 10.1210/endo-102-1-330 |
| Popis: | A partially purified preparation of hydroxy-indole-O-methyltransferase (HIOMT) from bovine pineal was shown to O-methylate estradiol-17β (E2). The HIOMT preparation was incubated with E2 and [3H]-S-adenosylmethionine (SAM). The [3H]-3 methyl-ether of estradiol [MeO-E2] produced was identified by thin layer chromatography (TLC) and crystallization to constant 3H/14C ratio in the presence of [14C]-Me0-E2 and unlabeled MeO-E2 standards. The kinetics of the enzyme reaction for melatonin formation from N-acetylserotonin (NAS) and for MeO-E2 were compared. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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