Linked Life Data

2822441

Source:http://linkedlifedata.com/resource/pubmed/id/2822441

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-12-14
pubmed:abstractText
The dephosphorylation of adenine nucleotides and their analogues by ectonucleotidases on the guinea-pig urinary bladder was studied using HPLC. The rate of dephosphorylation of each analogue was compared with its pharmacological potency at causing contraction. ATP, ADP and AMP were rapidly dephosphorylated, and substitution on the purine ring did not affect the rate of breakdown. The ectonucleotidases showed stereoselectivity towards the ribose moiety and towards the polyphosphate chain. In general, methylene isosteres of the nucleotides, and analogues in which one of the oxygen atoms on the terminal phosphate had been replaced, were resistant to degradation. None of the analogues that were readily dephosphorylated are more potent than ATP, and most but not all of the analogues resistant to degradation are more potent than ATP, suggesting that while resistance to degradation does not in itself confer high potency, susceptibility to degradation does limit the potency of ATP and its degradable analogues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-2999
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
141
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
123-30
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
The structure-activity relationships of ectonucleotidases and of excitatory P2-purinoceptors: evidence that dephosphorylation of ATP analogues reduces pharmacological potency.
pubmed:affiliation
Department of Pharmacology, University of London, King's College, Strand.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't