Abstract
NISHIHIRA, J., ISHIBASHI, T., IMAI, Y. and MURAMATSU, T. Purification and Characterization of the Specific Binding Protein for Platelet Activating Factor (1-O-Alkyl-2-Acetyl-sn-Glycero-3-Phosphocholine) from Human Platelets. Tohoku J. exp. Med., 1985, 147 (2), 145-152 The binding protein to platelet activating factor (PAF) was solubilized with 2% Triton X-100 from human platelet membranes and purified approximately 23-fold by sequential chromatography on DEAE-cellulose, CM-cellulose and Sephadex G-200. The final preparation migrated as a single protein band correspoding to a radioactive peak of [3H] PAF bound on polyacrylamide disc gel electrophoresis. The molecular weight of the native form of the binding protein was estimated to be approximately 160, 000 daltons by Sephadex G-200 column chromatography, and its isoelectric point was near 8.0. Exposure of the platelet membranes to an excess of unlabeled PAF diminished the binding of [3H] PAF.
