Metabolism of estradiol by uterine peroxidase: nature of the water-soluble products.

Abstract:

:The nature of the water-soluble products formed by incubating labelled estradiol with uterine peroxidase in the presence of H2O2 and tyrosine was examined by two-dimensional thin-layer chromatography and high voltage electrophoresis. It was shown that the steroid and amino acid were associated in a 1:2 or 1:3 ratio and evidence was provided by 3H-exchange for the interaction of tyrosine with ring A of estradiol at C-2 and C-4. The possible role of estrogen-induced peroxidase in the uterus in vivo is discussed.

journal_name

Steroids

journal_title

Steroids

authors

Jellinck PH,McNabb T

doi

10.1016/0039-128x(77)90072-1

subject

Has Abstract

pub_date

1977-04-01 00:00:00

pages

525-37

issue

4

eissn

0039-128X

issn

1878-5867

pii

0039-128X(77)90072-1

journal_volume

29

pub_type

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