Abstract
The interaction of A 1 myelin basic proteins and P 1, P 2 peripheral nerve basic proteins with different lipids has been studied at the air-water interface. Measurement of the change in surface pressure showed a highly specific interaction of A 1 basic protein with negatively charged lipids of myelin such as cerebroside sulphate. Neutral lipids such as lecithin, cholesterol and cerebrosides show markedly less affinity for the A 1 basic protein. The P 1 and P 2 basic proteins did not show specificity to this extent. Measurement of the surface radioactivity, using 131I-labelled A 1 basic protein, showed that the amount of A 1 basic protein bound to cerebroside sulphate monolayers parallels the pressure increase. The observed specificity, the effects of different solutes, differences in fatty acid chain length of the lipids and the increase in area at constant pressure demonstrate that ionic and hydrophobic forces are involved in the interaction of A 1 basic protein and lipids.
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