Linked Life Data

7394859

Source:http://linkedlifedata.com/resource/pubmed/id/7394859

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1980-9-23
pubmed:abstractText
The mitochondrial fraction of diethylstilbestrol-treated rat uteri, known to contain an estrogen-induced peroxidase, was able to catalyze the release of 3H2O from either [2-3H]- or [4-3H]estradiol. Hydrogen peroxide added to this system increased the yield of 3H2O but had no effect on mitochondrial preparations from ovariectomized rat uteri having only very low peroxidase activity. The reaction was inhibited by catalase and also occurred with lactoperoxidase in the presence of H2O2 but 2-hydroxyestradiol was not detected in any of these experiments. Under similar conditions, tyrosinase catalyzed the formation of the catechol estrogen with loss of 3H from [2-3H]- or [2,4,6,7-3H]- but not [4-3H]- or [6,7-3H]estradiol. It is proposed that the formation of 3H2O from 3H-labeled estradiol in the estrogen-treated rat uterus may occur by a peroxidative mechanism which does not necessarily result in hydroxylation of the steroid.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0039-128X
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
579-89
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Formation of 3H2O from [2-3H]- and [4-3H] estradiol by rat uteri in vitro: possible role of peroxidase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.