Bitbol M, Dempsey C, Watts A, Devaux P F
Department of Biochemistry, University of Oxford, England.
FEBS Lett. 1989 Feb 13;244(1):217-22. doi: 10.1016/0014-5793(89)81196-2.
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 (T1) 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 maintenance of PS in the inner monolayer of the erythrocyte membrane during the whole life-span of this cell.
来自人红细胞的血影蛋白可与二肉豆蔻酰磷脂酰胆碱（DMPC）以及二肉豆蔻酰磷脂酰丝氨酸-二肉豆蔻酰磷脂酰胆碱（DMPS:DMPC，质量比1:1）的双层分散体结合。然而，在含有氘代DMPC或DMPS的两种脂质1:1混合物中，通过极性头部基团特异性氘代的DMPC或DMPS的氘四重分裂测量，未检测到结合的血影蛋白对脂质头部基团构象有任何影响。血影蛋白既不影响DMPS:DMPC混合物的相变，也不影响氘代DMPS头部基团的自旋晶格弛豫时间（T1）。这些结果表明血影蛋白与磷脂酰丝氨酸之间不存在强烈相互作用，并排除了血影蛋白在该细胞的整个生命周期内负责维持红细胞膜内单层中PS的可能性。
