The lysis of cells by complement requires only the terminal components C5, C6, C7, C8 and C9 and is initiated by the cleavage of C5 to C5b. Sequential addition of C6, C7, C8, and C9 to C5b leads to the formation of the membrane attack complex (MAC)' which, when inserted into the lipid bilayer, can form transmembrane pores (1-5). It is well known that when complement of one species is activated on homologous erythrocytes, lysis is much less efficient than when it is activated on other species of cell, and even among different heterologous cell species the lytic efficiency may be very different. It has long been known that the basis of this variable lytic efficiency is found, at least in part, at the C8 and/or C9 step (6-9). More recently, specific membrane proteins have been described that appear to protect cells from homologous complement . The first of these to be described was the decayaccelerating factor (DAF), a membrane protein of -70 kD molecular mass (10). This protein interferes with the assembly of the C3 converting enzymes both of the classical and alternative pathway (10, 11) and therefore it has only indirect effects on the cell lytic mechanism. A further membrane protein that does restrict homologous lysis, and that has been described both as the C8-binding protein (C8bp) (7, 12) and as homologous restriction factor (HRF) (13), has also been isolated . It seems likely that both these descriptions apply to a single protein of 65 kD molecular mass. In addition, a 55/65-kD MAC-inhibiting protein (MIP) with the capacity to bind C8 and C9 has been identified both on human erythrocyte membranes and in normal human serum (14). The relationship ofthis to HRF/C8bp is not yet clear. Both DAF and HRF/C8bp are bound on cell membranes by a glycolipid anchor (15, 16) and can be eluted from the cell membrane, at least in part, by phosphatidylinositol-specific phospholipase C. These proteins also have the capacity when they are isolated from