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Interaction of erythrocyte spectrin with some nonbilayer phospholipids.

Bovine erythrocyte spectrin was found to interact with lysophosphatidylcholine and lysophospatidylserine what was detected by small changes of the intrinsic fluorescence of spectrin. Lysophosphatidylethanolamine in contrast to its diacyl, natural counterpart did not affect the intrinsic fluorescence of spectrin at all. Dioleoylphosphatidylethanolamine induced distinct changes in the intrinsic fluorescence from these induced by natural phosphatidylethanolamine suspensions. Our data may indicate an importance of the presence of both fatty acyl chains in phosphatidylethanolamine molecule and perhaps, its bilayer structure for the interaction of this phospholipid aggregates with spectrin.