Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1979-12-29
pubmed:abstractText
Two intracellular high-affinity, low-capacity estrogen-binding proteins, which have the characteristics of receptors, with equilibrium dissociation constants of 10(-10)M and 10(-9)M, have been observed in the human uterus. The higher-affinity protein (10(-10)M) appears to play the main role in activating end-organ response to estrogen stimulation. The role of the lower-affinity protein (10(-9)M) is uncertain. In a human postmenopausal uterine system without estrogen stimulation, Scatchard analysis of uterine cytosol partially purified by ammonium sulfate fractionation and incubated at 4 degrees C for 18 hours revealed only the higher-affinity receptor component (10(-10)M). In a post menopausal uterine system with estrogen priming (and in the premenopausal uterus) both the high- and low-affinity components were observed. Competition studies indicated that the receptors were specific for estradiol. The clinical significance of these findings is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0002-9378
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
135
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
799-803
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Estrogen-binding proteins in the human postmenopausal uterus.
pubmed:publicationType
Journal Article, Comparative Study