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Lipid perpendicular motion It is now apparent that some, and probably all, biological membranes are asymmetric with specific components being oriented to different surfaces of the membrane. , 1974). , 1975), ferritin-conjugated lectins (Nicolson and Singer, 1971, 1974; Nicolson, 1976c), ferritin-avidin complexes (Heitzmann and Richards, 1974) and, in the case of enzymes, histochemical localization (Marchesi and Palade, 1967; Porter and Bernacki, 1975). Singer and Nicolson (1972) proposed that the asymmetry of glycoproteins found in a variety of cells was probably due to their amphipathic structure which should make trans-membrane rotations or "flip-flop" energetically unfavorable.

Associations between oligosaccharides can be quite strong and are cooperative in many systems (Rees, 1969). , 1976). 2. 4). , 1974). 4). If proteins are sequestered into fluid lipid domains, their dynamic display would be limited to only those regions. Alternatively, if they associate preferentially with solid phase lipids, their mobility would be impeded because of a more viscous lipid matrix, and they would also be limited to solid phase lipid regions. Thus, the dynamics and topographic display of membrane proteins may well be controlled, in part, by their associations with other proteins or with specific lipids in fluid or solid phases.

The movement of integral membrane proteins or protein complexes can also 28 be detected by freeze-cleavage electron microscopy. A limitation here, as with other ultrastructural techniques, is that the same sample cannot be followed dynamically. , 1975a). , 1972; Pinto da Silva and Nicolson, 1974). , 1972), probably in association with the so called band III erythrocyte membrane glycoproteins (see Pinto da Silva and Nicolson, 1974). , 1975). , 1975). 2. Ligand-induced redistribution of cell surface components The ability of multivalent ligands such as antibodies (reviews, Unanue and Karnovsky, 1973; Edidin, 1974; Loor, 1976) and plant lectins (Nicolson, 1974; 1976a,b,c) to induce lateral movement and topographic rearrangement of cell surface receptors has been demonstrated in numerous laboratories using a wide range of cell types.

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