Linked Life Data

7758470

Source:http://linkedlifedata.com/resource/pubmed/id/7758470

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-6-27
pubmed:abstractText
Using the radioligand [1,2,6,7-3H]aldosterone ([3H]aldosterone), specific binding sites for aldosterone were identified and characterized in microsomal preparations from porcine liver. The maximum binding capacity is approximately 700 fmol x mg-1 microsomal protein. The reversible binding of [3H]aldosterone was saturable and Scatchard analysis revealed two apparent dissociation constants (Kd), Kd1 < or = 11 nM and Kd2 = 118 nM. Binding was optimal at pH 7.2, thermolabile, and was reduced by more than 70% when membrane vesicles were pretreated with trypsin. Binding was selective for aldosterone with cortisol being a weak agonist at 1000-fold higher concentrations only. Among those detergents tested to optimize conditions for solubilization, n-octylglucoside (75 mM) was most favorable and solubilized 25% of the radioligand-binding protein complex in the undissociated form. These binding sites have unique pharmacological properties, which are similar to those found for aldosterone membrane binding in human lymphocytes and pig kidney, and for rapid aldosterone effects on sodium-proton exchange.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
229
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
736-40
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Characterization and solubilization of novel aldosterone-binding proteins in porcine liver microsomes.
pubmed:affiliation
Medizinische Klinik, Klinikum Innenstadt, University of Munich, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't