Methylation of estradiol-17β by a partially purified preparation of bovine pineal hydroxy-indole-o-methyltransferase

Judith Weisz; Laura V. O’Brien; Tom Lloyd

doi:10.1210/endo-102-1-330

Methylation of estradiol-17β by a partially purified preparation of bovine pineal hydroxy-indole-o-methyltransferase

Judith Weisz, Laura V. O’Brien, Tom Lloyd

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Abstract

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.

Original language	English (US)
Pages (from-to)	330-333
Number of pages	4
Journal	Endocrinology
Volume	102
Issue number	1
DOIs	https://doi.org/10.1210/endo-102-1-330
State	Published - Jan 1978

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Endocrinology

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title = "Methylation of estradiol-17β by a partially purified preparation of bovine pineal hydroxy-indole-o-methyltransferase",

abstract = "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.",

author = "Judith Weisz and O{\textquoteright}Brien, {Laura V.} and Tom Lloyd",

year = "1978",

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doi = "10.1210/endo-102-1-330",

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T1 - Methylation of estradiol-17β by a partially purified preparation of bovine pineal hydroxy-indole-o-methyltransferase

AU - Weisz, Judith

AU - O’Brien, Laura V.

AU - Lloyd, Tom

PY - 1978/1

Y1 - 1978/1

N2 - 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.

AB - 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.

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Methylation of estradiol-17β by a partially purified preparation of bovine pineal hydroxy-indole-o-methyltransferase

Abstract

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