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The murine macrophage Fc receptor for IgG2b is lipid dependent
The plasma membrane Fc receptor for IgG2b on P388D1 cells, solubilized by detergent, was inactivated by incubation with phospholipase C. Soluble Fc receptor activity could be restored by the addition of liposomes of either phosphatidylethanolamine or phosphatidylinositol. The reconstituted Fc receptor was trypsin sensitive. These data indicate that Fc receptor binding of IgG2b results from the concerted action of membrane lipid and protein.
The plasma membrane Fc receptor for IgG2b on P388D1 cells, solubilized by detergent, was inactivated by incubation with phospholipase C. Soluble Fc receptor activity could be restored by the addition of liposomes of either phosphatidylethanolamine or phosphatidylinositol. The reconstituted Fc receptor was trypsin sensitive. These data indicate that Fc receptor binding of IgG2b results from the concerted action of membrane lipid and protein.