Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1979-2-23
pubmed:abstractText
Incubation of bovine adrenocortical membranes with corticotropin and 5-guanylylimidodiphosphate produced a state of adenylate cyclase (ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1) with maximal catalytic activity and an increased sensitivity to inhibition by adenosine. Due to metabolism of adenine nucleotides during adenylate cyclase assays a quantitative assessment of the nature of this inhibition was not possible. However, when determined at 0.2--1.0 mM MgATP2-, half-maximal inhibition of the basal and maximally active states of the enzyme was observed at adenosine concentrations of 210--330 and 70--90 micrometer, respectively. The inhibition appeared to be partially competitive, suggesting that the nucleoside may act as an allosteric negative effector which reduces the affinity of the active site for substrate. Adenosine was 5--6 times more potent as an inhibitor of adrenal adenylate cyclase than 2-chloroadenosine. Adenosine deaminase abolished the inhibitory effect of the nucleoside, whilst theophylline had no effect on activity either in the absence or presence of adenosine.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
526
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
605-12
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Inhibition of bovine adrenocortical adenylate cyclase activity by adenosine.
pubmed:publicationType
Journal Article, Comparative Study