Linked Life Data

1906014

Source:http://linkedlifedata.com/resource/pubmed/id/1906014

Statements in which the resource exists.
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pubmed-article:1906014pubmed:abstractTextHuman platelets, prelabeled with [32P]phosphate were treated with tetradecanoylphorbol acetate (TPA) for 5 min at 37 degrees C. Phosphorylation of the components of adenylyl cyclase was determined in membranes using specific antibodies against G-proteins and the catalytic moiety. Less than 0.01 mol of [32P]phosphate/mol could be detected in immunoprecipitates using antibodies against sequences within the alpha-subunit of the GTP binding protein Gi. TPA, however, caused the incorporation of 0.67-1.1 mol of [32P]phosphate per mol of catalyst while 0.13-0.2 mol were found in the absence of TPA. Lack of modification of the alpha-subunit of Gi was also indicated by the results of reconstitution experiments with purified Gi alpha from bovine brain: adenylyl cyclase in membranes from untreated platelets was significantly more inhibited by added G1 alpha, than that from TPA treated cells. While beta, gamma-subunits were like-wise inhibitory no difference dependent on platelet-pretreatment could be observed.lld:pubmed
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pubmed-article:1906014pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:1906014pubmed:articleTitleChemical and functional analysis of components of adenylyl cyclase from human platelets treated with phorbolesters.lld:pubmed
pubmed-article:1906014pubmed:affiliationDepartment of Physiological Chemistry, University of Würzburg, Medical School, Germany.lld:pubmed
pubmed-article:1906014pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1906014pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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