Linked Life Data

885844

Source:http://linkedlifedata.com/resource/pubmed/id/885844

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1977-9-22
pubmed:abstractText
Guanyl-5'-yl-(alpha,beta-methylene)di[gamma-32P]phosphonate (Gp-(CH2)pp) is not hydrolyzed by rat liver membranes under conditions in which GTP and guanyl-5'-yl imidodiphosphate (Gpp(NH)p) are hydrolyzed. Gp(CH2)pp activates adenylate cyclase in hepatic membranes with characteristics similar to those of Gpp(NH)p activation but with lower potency and effectiveness. The analogs, although with lower potency than GTP, also share the ability to change the glucagon receptor from a high to a low affinity state. Both Gp(CH2)pp and Gpp(NH)p stimulate adenylate cyclase activity following a lag period of about 1 min addition of GTP after steady state rates are achieved results in reduction in the rate following a lag period of 6 min from the time of addition of GTP. Pretreatment of the enzyme with Gpp(NH)p or Gp(CH2)pp, followed by washing the membranes, leads to a high activity state of the enzyme which slowly decays in rate unless the analogs are continuously present in the medium. These data suggest that the guanosyl nucleotide analogs act on the enzyme system by a slowly reversible process that possibly reflects slow binding and dissociation from different transition states of the enzyme system and suggest that activation of adenylate cyclase by GTP, Gpp(NH)p, and Gp(CH2)pp does not involve covalent modification of the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
252
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5180-2
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Reversible activation of hepatic adenylate cyclase by guanyl-5'-yl-(alpha,beta-methylene)diphosphonate and guanyl-5'-yl imidodiphosphate.
pubmed:publicationType
Journal Article