By G.H. Bourne (ed.), J.F. Danielli (ed.)
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First we note that in most FRAP studies fluorescently labeled antibodies, antibody fragments, lectins, or other macromolecular ligands have been used to label the membrane proteins. As previously stated, the D values and percentage recovery are consistently lower than for integral proteins in reconstituted systems or for rhodopsin in the disk membrane. , 1982). , 1979) and postinactivation recovery of functional activity (Poo, 1982). Using these methods the diffusion coefficients for Con A and acetylcholine (ACh) receptors in embryonic Xenopus muscle cells were estimated to be in the range of 1-4 X cm2/second.
In bilayers consisting of a binary mixture of cholesterol and dimyristoyl phosphatidylcholine the coexistence of solid and fluid regions can dramatically influence long-range diffusion of fluorescent lipids (Rubenstein et a l . , 1980; Owicki and McConnell, 1980). Measured D values for the solid-fluid mixture differ by more than an order of magnitude from theoretical microscopic D values in either phase. Klausner and Wolf (1980) find that certain fluorescent lipid analogs are largely immobile (mobile fraction 25%) in a solid-fluid mixture of di-C,,- and di-(=,,-lecithin while other analogs are almost 100% mobile, and they interpret this as due to selective partitioning of the different probes into either solid or fluid domains.
1980), thyrotropin receptors (Avivi et a l . , 1981), p-adrenoreceptors (Henis et a l . , 1978). Oliver and Berlin (1982) discuss several cases of ligand-induced receptor migration in leukocytes and propose an “entrainment” of the ligand-receptor complexes in actively propagated membrane ‘‘waves. ” There is also the distinct possibility that lectin receptors may globally modulate their own mobility by signaling cytoplasmic attachments upon binding (Henis and Elson, 198I ) . Aside from these specific and sometimes biologically important effects, we are concerned with a possible nonspecific effect due to ligand binding.
