Showing papers by "Robert J. Lefkowitz published in 1972"
TL;DR: A protein that binds catecholamines with a specificity parallel to that of their in vivo effects on cardiac contractility was solubilized from a microsomal fraction of canine ventricular myocardium and purified 500 to 800-fold with conjugates of norepinephrine linked to agarose beads.
Abstract: A protein that binds catecholamines with a specificity parallel to that of their in vivo effects on cardiac contractility (isoproterenol > epinephrine or norepinephrine > dopamine > dihydroxyphenylalanine) was solubilized from a microsomal fraction of canine ventricular myocardium. The binding protein was purified 500 to 800-fold by solubilization and subsequent affinity chromatography with conjugates of norepinephrine linked to agarose beads. Purified beta-adrenergic binding protein exists in two forms, corresponding to molecular weights of 40,000 and 160,000. The purified material has a single association constant, 2.3 x 10(5) liters/mol (as compared to two association constants, 10(7) and 10(6) liters/mol, for the binding protein in particulate form) but retains the identical binding specificity for beta-adrenergic drugs and antagonists.
92 citations
TL;DR: A solubilized preparation of cat ventricular myocardium freed of detergent by DEAE-cellulose chromatography, contained both β-adrenergic receptors and adenylate cyclase, which required addition of phosphatidylinositol but finding of [3H]-norepinephrine to receptors did not.
34 citations