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HIGH AFFINITY ACCEPTOR SITES IN GUINEA PIG BRAIN FOR [ 3 H]52770 RP, A PAF ANTAGONIST
Author(s) -
LEVY C.,
BAUDOUY N.,
BRUN V.,
GOZE O.,
ZUNDEL J.L.,
BLANCHARD J.C.,
LADURON P.M.
Publication year - 1989
Publication title -
fundamental and clinical pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.655
H-Index - 73
eISSN - 1472-8206
pISSN - 0767-3981
DOI - 10.1111/j.1472-8206.1989.tb00028.x
Subject(s) - guinea pig , antagonist , chemistry , pharmacology , endocrinology , medicine , biochemistry , receptor
Summary— [ 3 H]52770 RP, a PAF antagonist, was found to bind with high affinity and in a reversible manner on specific and saturable binding sites in guinea pig cortical membranes. Scatchard analysis revealed the presence of one class of binding sites with an equilibrium dissociation constant of 0.38 nM and a B max of 1190 fmol/mg protein. However, these binding sites did not correspond to the PAF receptors described with this ligand in platelet plasma membranes; indeed, PAF and its analogs were unable to displace [ 3 H]52770 RP binding in guinea pig brain. Therefore, one may conclude that [ 3 H]52770 RP in guinea pig brain labels acceptor or recognition sites, rather than true receptor sites.