Isolation of Fc receptor shed from pig lymphocytes by a temperature shift.
Lymphocytes obtained from pig blood by gradient centrifugation were subjected to a temperature shift (4 to 37 degrees C). The proteins released from the plasma membrane were fractionated by affinity chromatography using immunoglobulin G immobilized on fine polyamide particles. The main component liberated from the adsorbent by diethylamine buffer (pH 11.5) exhibited an apparent Mr of 18000-20000 in SDS-polyacrylamide gel electrophoresis. This crude receptor preparation possessed a substantially higher affinity to immobilized immunoglobulin G than to immobilized Fab fragment and inhibited significantly the binding of labeled immunoglobulin G to pig lymphocytes.
D000818:Animals; D001667:Binding, Competitive; D002462:Cell Membrane / Q000276:immunology; D002846:Chromatography, Affinity / Q000379:methods; D007141:Immunoglobulin Fc Fragments / Q000276:immunology; D007074:Immunoglobulin G; D008214:Lymphocytes / Q000276:immunology*; D011961:Receptors, Fc / Q000302:isolation & purification*; D013552:Swine; D013696:Temperature
D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D011961:Receptors, Fc