Platelet-associated IgG is a specific protein.
The immunoglobulin binding to normal human platelets (PaIgG) was isolated on cell columns in which platelets or their membranes were attached via concanavalin A to an inert support matrix. Normal human IgG isolated from pooled serum was applied to the cell columns. The absorbed material which was eluted at low pH with a buffer of high ionic strength was immunologically and biochemically pure IgG. When the nonadherent IgG of the first passage through the platelet cell column was reapplied a second time virtually no IgG was retained. Isoelectric focusing on urea SDS polyacrylamide gels revealed only 2 major bands with pIs of 8.2 and 8.4 whereas the precolumn IgG contained a wide range of molecular species with pIs ranging from less than 6.0 to 9.0.
D001792:Blood Platelets / Q000276:immunology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007122:Immunoelectrophoresis; D007074:Immunoglobulin G / Q000032:analysis*; D007525:Isoelectric Focusing; D008970:Molecular Weight; D009994:Osmolar Concentration
D007074:Immunoglobulin G