Electron microscopic observation of the aggregation of membrane proteins in human erythrocyte by melittin.
Electron microscopic observation of the aggregation of membrane proteins in human erythrocyte by melittin.
复制标题
蜂毒肽对人红细胞膜蛋白聚集的电镜观察。
DOI:
10.1016/0005-2736(90)90124-7
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发表时间:
1990
期刊:
影响因子:
--
通讯作者:
Cherry,RJ
中科院分区:
文献类型:
--
作者:
Hui,SW;Stewart,CM;Cherry,RJ
Human erythrocytes and erythrocyte ghost membranes were treated with native and modified melittins, up to 250 nmol/mg membrane protein. Native melittin induced aggregation of intramembranous particles (IMPs, observed by freeze-fracture electron microscopy), and created large, smooth bilayer areas devoid of IMP. The degree of IMP aggregation increased with increasing concentration of melittin, corresponding to hemolysis results. Membrane ghosts were slightly more susceptible to IMP aggregation than membranes on intact cells. The potency of inducing IMP aggregation was ranked in the order of: native melittin > acetylated melittin > succinylated melittin = 0. The concentration range of melittin which caused IMP aggregation corresponded to that which caused the immobilization of band 3 proteins as detected by measurement of rotational mobility by transient dichroism (Dufton et al. (1984) Eur. J. Biophys. 11, 17–24). Because both IMP aggregation and band 3 protein immobilization decreased with decreasing positive charge of the melittins used, the nature of melittin-protein interaction is likely to be at least in part electrostatic in the case of human erythrocyte membranes. Possible roles of IMP aggregation and the consequent creation of ‘exposed’ bilayer areas in the cytotoxic reaction of melittins are discussed.