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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
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pubmed:dateCreated |
1981-12-15
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pubmed:abstractText |
The enzyme kinetics of estrogen 2-hydroxylase from rat liver microsomes has been investigated using two radiotracer methods. The conversion of [4-14C]estradiol to [4-14C]2-hydroxyestradiol by microsomes was examined by isolation of the catechol estrogen. [6,7-3H]2-Hydroxyestradiol was prepared and added at the end of the incubation as a recovery marker for quantitation. Initial velocity conditions of less than 10% product formation were established. The enzyme kinetics for estrogen 2-hydroxylase from male rat liver follows classical Michaelis-Menten kinetics producing a linear Lineweaver-Burk plot. The apparent Km for estradiol under these conditions was 2.2 microM; the Vmax for freshly prepared microsomes was 5.0 nmol/mg/min while that for microsomes stored at -70 degrees C was 0.51 nmol/mg/min. On the other hand, estrogen 2-hydroxylase from female rat liver microsomes did not follow Michaelis-Menten kinetics and yielded a nonlinear double reciprocal plot. Analogous kinetic data were obtained with another radiotracer assay measuring the release of 3H2O from [2-3H]estradiol. Thus, the estrogen 2-hydroxylases of male and female rat liver differ in enzyme kinetic properties. The upwardly curving Lineweaver-Burk plot of the kinetic data of the female rat liver microsomes suggests that more than one binding site for estradiol may exist on this enzyme complex and/or that this particular estrogen 2-hydroxylase system exhibits cooperative effects.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 CYP1A1,
http://linkedlifedata.com/resource/pubmed/chemical/Estrogens,
http://linkedlifedata.com/resource/pubmed/chemical/Steroid Hydroxylases,
http://linkedlifedata.com/resource/pubmed/chemical/estrogen 2-hydroxylase
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
256
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10239-42
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7287706-Animals,
pubmed-meshheading:7287706-Carbon Radioisotopes,
pubmed-meshheading:7287706-Cytochrome P-450 CYP1A1,
pubmed-meshheading:7287706-Estrogens,
pubmed-meshheading:7287706-Female,
pubmed-meshheading:7287706-Kinetics,
pubmed-meshheading:7287706-Male,
pubmed-meshheading:7287706-Microsomes, Liver,
pubmed-meshheading:7287706-Rats,
pubmed-meshheading:7287706-Rats, Inbred Strains,
pubmed-meshheading:7287706-Sex Factors,
pubmed-meshheading:7287706-Steroid Hydroxylases
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pubmed:year |
1981
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pubmed:articleTitle |
Kinetics of rat liver microsomal estrogen 2-hydroxylase. Evidence for sex differences at initial velocity conditions.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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