Linked Life Data

2163471

Source:http://linkedlifedata.com/resource/pubmed/id/2163471

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1990-8-7
pubmed:abstractText
Estradiol and 2-hydroxyestradiol with 3H at different positions in rings A, B or D were incubated with lactoperoxidase without added H2O2 and their oxidative transformation was followed by transfer of 3H into 3H2O. With estradiol, 3H loss from different positions in the aromatic ring was almost equal and also occurred to a lesser extent from the alicyclic portion of the molecule. Glutathione had less effect on the formation of 3H2O for the aromatic ring of estradiol than from that of the catechol estrogen where it increased the yield 6-fold. The rate of 3H loss was also very much greater from tritiated 2-hydroxyestradiol than from estradiol and NADPH was inhibitory with both steroids. Conditions for the release of 3H from estradiol and 2-hydroxyestradiol by peroxidase as well as the effect of some biochemical inhibitors were also investigated. The possible contribution of peroxidative formation of 3H2O during the radiometric assay for catechol estrogen biosynthesis by tissue monooxygenases is discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-4731
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
705-10
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Peroxidase-catalyzed displacement of tritium from regiospecifically labeled estradiol and 2-hydroxyestradiol.
pubmed:affiliation
Department of Biochemistry, Queen's University, Kingston, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't