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Specific binding of antibodies to platelet‐activating factor (PAF) as demonstrated by thin‐layer chromatography/Immunostaining
Author(s) -
Karasawa Ken,
Satoh Noriko,
Hongo Toshio,
Nakagawa Yasuhito,
Setaka Morio,
Nojima Shoshichi
Publication year - 1991
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02536514
Subject(s) - phosphatidic acid , phosphatidylserine , chemistry , platelet activating factor , cardiolipin , phosphatidylethanolamine , phosphatidylcholine , phosphatidylinositol , bovine serum albumin , phospholipid , phosphatidylglycerol , immunostaining , sphingomyelin , biochemistry , biology , membrane , signal transduction , immunology , immunohistochemistry
The specificity of rabbit antibodies produced by injection of 1‐ O ‐(15'‐carboxypentadecyl)‐2‐ N,N ‐dimethylcar‐bamoyl‐ sn ‐glycero‐3‐phosphocholine bovine serum albumin (BSA) conjugates was examined by a thin‐layer chromatography (TLC)/immunostaining method. Phosphatidylcholine (PC), lysophosphatidylcholine (lysoPC), lyso platelet‐activating factor (lysoPAF), phosphatidylethanolamine (PE), phosphatidylglycerol (PG), phosphatidylserine (PS), sphingomyelin (SM), phosphatidylinositol (PI), phosphatidic acid (PA) and cardiolipin (CL) were not immunostained. Among several synthetic PAF‐related compounds, the antibodies only bound to PAF agonists which have the activity to induce washed rabbit platelet aggregation. The results suggest that the binding sites of the antibodies on the PAF molecule are the acetyl group at the sn ‐2 position and the choline moiety at the sn ‐3 position of glycerol, both of which are essential for exerting the biological function of PAF and for binding to the PAF receptors located on cellular membranes.