[The receptor of adenosine-dephosphate on the human platelet membrane (author's translation)].
The binding of 14C-ADP on the isolated platelet membrane is a saturable and reversible phenomenon which seems to implicate a protein only partially solubilised by Triton X-100. The binding is strongly reduced by mersalyl, which is known to inhibit the ATPase activity of the thrombosthenin i.e. the platelet contractile protein; this protein could be involved in the mechanism of binding of ADP on the platelet membrane. Platelets not aggregated by ADP from patients with Glanzmann's thrombasthenia, have a normal binding of 14C-ADP which is also strongly reduced by mersalyl.
D000244:Adenosine Diphosphate / Q000494:pharmacology*; D001792:Blood Platelets / Q000187:drug effects*; D001798:Blood Proteins / Q000037:antagonists & inhibitors; D002250:Carbon Radioisotopes; D002462:Cell Membrane / Q000187:drug effects; D006801:Humans; D007700:Kinetics; D008634:Mersalyl / Q000494:pharmacology; D010042:Ouabain / Q000494:pharmacology; D011092:Polyethylene Glycols; D011696:Purpura, Thrombocytopenic / Q000235:genetics; D011955:Receptors, Drug; D012995:Solubility; D013577:Syndrome
D001798:Blood Proteins; D002250:Carbon Radioisotopes; D011955:Receptors, Drug; D011092:Polyethylene Glycols; D010042:Ouabain; D008634:Mersalyl; D000244:Adenosine Diphosphate
Récepteur de l'adénosine-dephosphate à la surface des plaquettes sanguines humaines