Boyer M, Feinberg J, Hue H K, Capony J P, Benyamin Y, Roustan C
Centre de Recherches de Biochimie Macromoléculaire (C.N.R.S.), Unité N. 249 (I.N.S.E.R.M.), Montpellier, France.
Biochem J. 1987 Dec 1;248(2):359-64. doi: 10.1042/bj2480359.
The implication of part of the C-terminal of actin (within the 285-375 sequence) in the interaction of serum gelsolin was investigated by the use of specific antibodies. These antibodies were directed against two or three discrete epitopes, one of which was specific for skeletal-muscle actin. Some of these epitopes were found to be near the serum gelsolin-actin interface. Thus it can be assumed that part of the C-terminal of actin is exposed at the barbed end of the actin filament. The interaction between tropomyosin and actin was also studied.
通过使用特异性抗体研究了肌动蛋白C末端的一部分(在285 - 375序列内)在血清凝溶胶蛋白相互作用中的作用。这些抗体针对两个或三个离散表位,其中一个对骨骼肌肌动蛋白具有特异性。发现其中一些表位靠近血清凝溶胶蛋白 - 肌动蛋白界面。因此可以推测肌动蛋白C末端的一部分暴露在肌动蛋白丝的带刺末端。还研究了原肌球蛋白与肌动蛋白之间的相互作用。