The bromination of alpha-ergokryptine, a genuine ergot alkaloid of the peptide type, in position 2 of the indol nucleus to 2-bromo-alpha-ergokryptine is described. Its transformation to the methanesulfonate led to the prolactin inhibitor bromocriptine-methanesulfonate, Parlodel.
View Article and Find Full Text PDFAn iodine-labeled beta-adrenergic inhibitor ((125)l-hydroxybenzylpindolol) binds specifically to a site on turkey erythrocyte membranes. A series of beta-adrenergic agonists and inhibitors compete for this binding site, with apparent affinities paralleling biological effectiveness as activators or inhibitors of catecholaminestimulated adenylate cyclase. The activity of d-(+) agonists or inhibitors was 1 percent (or less) than that of the corresponding l-(-) isomers in competing for binding of the iodinated blocker as well as in affecting catecholamine-stimulated adenylate cyclase.
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