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Abstract
Characterization of specific vasopressin binding sites to rat hippocampal membranes has been assayed using tritiated lysine-vasopressin labelled on the tyrosyl residue. At 30°C specific [ 3H]vasopressin binding was saturable. The estimated equilibrium dissociation constant was 7.1 nM, the mean maximal binding capacity was 78 fmol/mg protein. Arginine-vasopressin has a high affinity ( K d = 2.8 nM) and dDAVP has a low affinity ( K d = 249 nM) for hippocampal synaptic membranes. (OH)AVP and Phe 2Orn 8VT are at least as active as AVP in inhibiting [ 3H]vasopressin binding. Adenylate cyclase was activated by VIP and inhibited by PIA, but not affected by lysine-vasopressin.
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