Specific arginine vasopressin binding in particulate membrane from rat aorta.
Arginine vasopressin (AVP) has been shown to have direct pressor effects on vascular smooth muscle. We have characterized a specific binding site for AVP in rat aorta membranes. We identified a specific binding site for AVP with a Kd of 1.6 nM and Bmax of 48 pM/mg protein. The time course, pH dependence, and temperature dependence were consistent with those found for other peptide receptors. Analogues of AVP competed with tritium labelled AVP for binding to the aortic vascular receptor in direct proportion to their pressor activities.
D000818:Animals; D001011:Aorta / Q000378:metabolism*; D001127:Arginine Vasopressin / Q000378:metabolism*; D001667:Binding, Competitive; D002413:Cations, Divalent / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008297:Male; D008566:Membranes / Q000378:metabolism; D009131:Muscle, Smooth, Vascular / Q000378:metabolism; D051381:Rats; D011945:Receptors, Angiotensin / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D017483:Receptors, Vasopressin; D013329:Structure-Activity Relationship; D013696:Temperature
D002413:Cations, Divalent; D011945:Receptors, Angiotensin; D011956:Receptors, Cell Surface; D017483:Receptors, Vasopressin; D001127:Arginine Vasopressin