Linked Life Data

818136

Source:http://linkedlifedata.com/resource/pubmed/id/818136

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1976-8-2
pubmed:abstractText
Turkey erythrocyte membranes contain beta-adrenergic-coupled adenylate cyclase systems that are modulated by guanine nucleotides. Incubation of membranes with Gpp (NH) p plus isoproterenol led to a persistently activated state ("holocatalytic state") of adenylate cyclase independent of agonist. Formation of this holocatalytic state was inhibited by conditions (4 degrees) or by compounds (e.g., GTP EDTA) that prevented Gpp (NH) p binding or that prevented binding of isoproterenol (e.g., propranolol). None of these agents, however, reduced activity of this activated state once it had been formed. The holocatalytic state, even though resistant to inhibition by propranolol, showed no change in receptor affinity or number of sites as determined by binding of 125I-HYP, a high affinity beta-adrenergic antagonist. Formation of the holocatalytic state, therefore, involves a modification of the adenylate cyclase system distal to the hormone receptor complex.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0095-1544
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
47-56
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Holocatalytic state of adenylate cyclase in turkey erythrocyte membranes: formation with guanylylimidodiphosphate plus isoproterenol without effect on affinity of beta-receptor.
pubmed:publicationType
Journal Article