INTERACTION OF ERYTHROCYTE SPECTRIN WITH SOME NONBILAYER PHOSPHOLIPIDS

Bovine erythrocyte spectrin was found to interact with lysophosphatidy lcholine and lysophospatidylserine what was detected by small changes of the intrinsic fluorescence of spectrin. Lysophosphatidylethanolamin e in contrast to its diacyl, natural counterpart did not affect the in trinsic fluorescence of spectrin at all. Dioleoylphosphatidylethanolam ine 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 ph osphatidylethanolamine molecule and perhaps, its bilayer structure for the interaction of this phospholipid aggregates with spectrin.