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The specificity of the binding of platelet activating factor (PAF) to anti‐PAF antibodies
Author(s) -
Smal Mary A.,
Baldo Brian A.,
Harle David G.
Publication year - 1990
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.300030406
Subject(s) - platelet activating factor , hapten , chemistry , antibody , phospholipid , thioether , stereochemistry , biochemistry , ether , platelet activating factor receptor , receptor , biology , immunology , organic chemistry , antagonist , membrane
Quantitative hapten inhibition experiments employing sheep anti‐PAF antibodies and selected PAF analogues were undertaken with the aim of defining the antigenic determinant structures complementary to the antibody combining sites. The most important fine structural features for inhibition of antibody binding to PAF were shown to be an acetyl group at position 2 of the phospholipid glycerol backbone and an ether group at position 1. Of the naturally occurring compounds, C 16 ‐ and C 18:1 ‐PAF proved to be the most potent inhibitors and more active than C 18 ‐PAF while phospholipids with a propionyl, butyryl or hexanoyl group at position 2 showed either weak or no inhibitory activity. The 1‐acyl, thioether and deoxy analogues proved inactive. Variations in the polar head group of PAF were found to be less critical with, for example, the dimethyl and ethanolamine derivatives retaining some activity. This antibody recognition pattern is very similar to that of the PAF receptor, although the antibodies appear to have a more specific requirement for an acyl linkage at position 2.