Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3-4
|
pubmed:dateCreated |
1989-3-2
|
pubmed:abstractText |
4-Hydroxyestradiol bearing a 3H label specifically at C-2 was prepared chemically and incubated with male rat liver microsomes or mushroom tyrosinase. A very high proportion (80-90%) of the 3H was displaced from the labeled steroid when either glutathione or N-acetylcysteine was present, and tyrosinase was shown not to require NADPH as cofactor for this reaction. In either case, only negligible amounts (less than 3%) of the 3H radioactivity were found associated with water-soluble adducts in contrast to 3H-labeled 2-hydroxyestradiol, which gave rise to about 25% of such products. The effect of ascorbic acid on the microsomal reaction with regiospecifically labeled estradiol, 2-hydroxyestradiol, and 4-hydroxyestradiol was also investigated, and the results are discussed in terms of the reactivity at different carbon atoms in ring A of the catechol estrogens. All the evidence points to conjugation of 4-hydroxyestradiol with glutathione or N-acetylcysteine at C-2 but not C-1 of this highly reactive catechol estrogen. Measuring the displacement of 3H as 3H2O from specific positions in the steroid ring provides a useful and sensitive method to assess the formation of adducts in cases where their isolation and characterization is particularly difficult.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-hydroxyestradiol-17 beta,
http://linkedlifedata.com/resource/pubmed/chemical/Catechol Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Estradiol,
http://linkedlifedata.com/resource/pubmed/chemical/Estrogens, Catechol,
http://linkedlifedata.com/resource/pubmed/chemical/Monophenol Monooxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0039-128X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
51
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
395-409
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:2851201-Animals,
pubmed-meshheading:2851201-Catechol Oxidase,
pubmed-meshheading:2851201-Estradiol,
pubmed-meshheading:2851201-Estrogens, Catechol,
pubmed-meshheading:2851201-Male,
pubmed-meshheading:2851201-Microsomes, Liver,
pubmed-meshheading:2851201-Monophenol Monooxygenase,
pubmed-meshheading:2851201-Rats,
pubmed-meshheading:2851201-Sulfhydryl Compounds,
pubmed-meshheading:2851201-Tritium
|
pubmed:articleTitle |
4-Hydroxyestradiol is conjugated with thiols primarily at C-2: evidence from regiospecific displacement of tritium by rat liver microsomes or tyrosinase.
|
pubmed:affiliation |
Department of Biochemistry, Queen's University, Kingston, Ontario, Canada.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|