INVITRO FORMATION OF A COMPLEX BETWEEN CYTOSKELETAL PROTEINS OF THE HUMAN-ERYTHROCYTE

被引:280
作者
UNGEWICKELL, E [1 ]
BENNETT, PM [1 ]
CALVERT, R [1 ]
OHANIAN, V [1 ]
GRATZER, WB [1 ]
机构
[1] UNIV LONDON KINGS COLL,MRC,CELL BIOPHYS UNIT,LONDON WC2R 2LS,ENGLAND
关键词
D O I
10.1038/280811a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The formation of a high-molecular weight complex between spectrin and F-actin depends on the presence of a third cytoskeletal constituent, protein 4.1. Electron microscopy shows that in this ternary complex the actin filaments are linked by bridges, which have the appearance of spectrin. The spectrin must be in the tetrameric state for such bridges to form: the dimer is evidently univalent, for it binds but forms no cross-links. G-actin also fails to form extended complexes. It is inferred that in the native cytoskeleton the spectrin is tetrameric and associated with 4.1 and probably oligomers of actin. © 1979 Nature Publishing Group.
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页码:811 / 814
页数:4
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