Isolation of a biologically active macrophage receptor for the third component of complement

C3b, the major cleavage fragment of the third component of complement (C3), has been demonstrated to bind to a specific receptor on various mammalian cells. Tissue-bound C3b receptors have also been demonstrated, most conclusively in renal glomeruli. On interaction with C3b, C3b receptors are thought to initiate cellular functions such as phagocytosis and to determine the fate of complement-fixing soluble and particulate immune complexes. We report here the isolation by affinity chromatography of a macrophage glycoprotein with an apparent molecular weight (MW) of approximately 64,000 that has properties expected of the C3b receptor. It is a cell-surface macromolecule (labelled with 125I and lactoperoxidase) which, in its isolated state, retains the ability to bind both C3 and C3b.