Linked Life Data

1003111

Source:http://linkedlifedata.com/resource/pubmed/id/1003111

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1977-2-24
pubmed:abstractText
In normal human kidney from adult males cytoplasmic components which bound 17beta-estradiol specifically and with high affinity were demonstrated by dextran-coated charcoal assay, sucrose gradient centrifugation and agar gel electrophoresis. The dissociation constant of the oestradiol-binder complex amounted to 2.2 +/- 0.1 x 10(-9) mol/l. The binding capacity was limited to 34.0 +/- 9.7 fmol/mg of cytosol protein. Sedimentation in sucrose gradient revealed the bulk of these components to be in the 4S region. The binding entities could be clearly separated from sex hormone-binding globulin by agar gel electrophoresis. The ligand specificity for binding to these components indicated a requirement for oestrogens. The fact that an excess of aldosterone had no competitive effect on oestradiol binding suggests that the oestrogen-binding sites are independent of mineralocorticoid receptors. It is concluded that the specific binding components in human kidney have the properties of oestrogen receptors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0340-076X
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
515-20
pubmed:dateRevised
2009-11-3
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Identification and partial characterization of specific oestrogen-binding components in human kidney.
pubmed:publicationType
Journal Article