Premium
[ 3 H]Vasopressin binding to rat hippocampal synaptic plasma membrane
Author(s) -
Barberis C.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80795-9
Subject(s) - vasopressin , dissociation constant , membrane , cyclase , arginine , neuropeptide , hippocampal formation , chemistry , adenylate kinase , binding site , biochemistry , arginine vasopressin receptor 1b , medicine , endocrinology , biophysics , vasopressin receptor , biology , amino acid , receptor
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 [ 3 H]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 2 Orn 8 VT are at least as active as AVP in inhibiting [ 3 H]vasopressin binding. Adenylate cyclase was activated by VIP and inhibited by PIA, but not affected by lysine‐vasopressin.