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Weak interaction of spectrin with phosphatidylcholine‐phosphatidylserine multilayers: A 2 H and 31 P NMR study
Author(s) -
Bitbol Michel,
Dempsey Christopher,
Watts Anthony,
Devaux Phillippe F.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81196-2
Subject(s) - spectrin , chemistry , phosphatidylserine , deuterium , bilayer , crystallography , lipid bilayer , monolayer , deuterium nmr , phospholipid , membrane , stereochemistry , nuclear magnetic resonance spectroscopy , cell , biochemistry , atomic physics , physics , cytoskeleton
Spectrin from human erythrocytes binds to bilayer dispersions of both DMPC and DMPS:DMPC (1:1, w/w). However, no effect of bound spectrin on the conformation of the lipid head groups, as measured from the deuterium quadrupolar splittings of DMPC or DMPS specifically deuterated in the polar head groups, was detected in 1:1 mixtures of the two lipids containing either deuterated DMPC or DMPS. Neither the phase transition of the DMPS:DMPC mixtures, nor the spin‐lattice relaxation time ( T 1 ) of the deuterated DMPS head group, was affected by spectrin. These results argue against any strong interaction of spectrin with phosphatidylserine and rule out the possibility that spectrin is responsible for the maintainance of PS in the inner monolayer of the erythrocyte membrane during the whole life‐span of this cell.