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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1983-12-21
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pubmed:abstractText |
Steroid glucuronidation was investigated in solubilized female rat and rabbit liver microsomes and in preparations of UDP-glucuronsyltransferase (UDPGT) activity resolved from these organelles. Solubilized rabbit liver microsomes possessed relatively high UDPGT activity towards estrone and beta-estradiol but not testosterone. Glucuronidation observed at the 3-OH position of beta-estradiol is 20-fold greater than at the 17-OH position. Estrone UDPGT activity, highly purified from rabbit liver microsomes, was active towards estrone and the 3-OH position of beta-estradiol but not towards testosterone (17-OH) or the 17-OH position of beta-estradiol. Thus, estrone UDPGT activity demonstrated essentially the same specificity for conjugation of the 3-OH position of beta-estradiol as observed in microsomes. Solubilized liver microsomes from female rats possessed approximately 4-fold more activity towards testosterone (17-OH) than estrone (3-OH). Rat liver microsomes formed about 2.5-fold more beta-estradiol 17-glucuronide than 3-glucuronide. Following a Chromatofocusing procedure where a gradient from pH 9-7 was employed, an eluant fraction was obtained that was enriched in estrone UDPGT activity relative to testosterone UDPGT activity. The fraction preferentially conjugated the 3-OH position of beta-estradiol. Two eluant fractions were obtained which demonstrated high levels of UDPGT activity towards testosterone and beta-estradiol but not estrone. Both fractions possessed a UDPGT activity that displayed a high degree of specificity for conjugation of the 17-OH position of beta-estradiol. A 17-OH steroid UDPGT was purified to apparent homogeneity from one of these fractions. These results suggest that separate UDPGT activity exists in female rat liver for the glucuronidation of the 3- and 17-OH positions of beta-estradiol. In female rabbit liver, beta-estradiol is predominantly conjugated at the 3-OH position by a single form of UDPGT.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0090-9556
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
426-32
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6138227-Animals,
pubmed-meshheading:6138227-Female,
pubmed-meshheading:6138227-Glucuronosyltransferase,
pubmed-meshheading:6138227-Microsomes, Liver,
pubmed-meshheading:6138227-Rabbits,
pubmed-meshheading:6138227-Rats,
pubmed-meshheading:6138227-Rats, Inbred Strains,
pubmed-meshheading:6138227-Species Specificity
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pubmed:articleTitle |
Steroid 3- and 17-OH UDP-glucuronosyltransferase activities in rat and rabbit liver microsomes.
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pubmed:publicationType |
Journal Article,
Comparative Study,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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