Inhibition of platelet [3H]-imipramine binding by human plasma protein fractions.
Inhibition of high-affinity [3H]-imipramine binding to platelet membranes by human plasma fractions and isolated plasma proteins was investigated. Several plasma proteins were found to contribute to the observed apparent inhibition and this contribution was assessed in terms of inhibitor units. Alpha 1 acid glycoprotein, high density and low density lipoprotein, IgG and alpha 1-antitrypsin were identified as effective non-specific inhibitors. Alpha-1-acid glycoprotein was confirmed to be the most potent plasma protein inhibitor. Cohn fractions were evaluated for the presence of the postulated endocoid of [3H]-imipramine binding site.
Strijewski
A
A
Psychopharmacology Unit, Clarke Institute of Psychiatry, Toronto, Ontario, Canada.
Chudzik
J
J
Tang
S W
SW
D001665:Binding Sites; D001792:Blood Platelets / Q000378:metabolism*; D001798:Blood Proteins / Q000494:pharmacology*; D002462:Cell Membrane / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007099:Imipramine / Q000097:blood*; D012701:Serotonin / Q000378:metabolism; D014316:Tritium
D001798:Blood Proteins; D014316:Tritium; D012701:Serotonin; D007099:Imipramine