Dabrowska R, Próchniewicz E, Drabikowski W
J Muscle Res Cell Motil. 1983 Feb;4(1):83-93. doi: 10.1007/BF00711959.
F-actin filaments are disrupted by the action of cytochalasin and glutaraldehyde. Muscle tropomyosin which is able to polymerize can protect F-actin against fragmentation caused by these two agents. This protective effect does not occur with nonpolymerizable, brain or carboxy-peptidase A-treated skeletal muscle tropomyosins. The protection of F-actin against the action of cytochalasin and glutaraldehyde takes place under conditions where the F-actin filaments are saturated with tropomyosin, that is, at a molar ratio of tropomyosin to actin of 1:7. It is suggested that nonpolymerizable tropomyosin lacks the protective ability because its binding to F-actin is considerably weaker than the polymerizable tropomyosin and does not saturate all of the binding sites on F-actin.
细胞松弛素和戊二醛的作用会破坏F-肌动蛋白丝。能够聚合的肌肉原肌球蛋白可以保护F-肌动蛋白免受这两种试剂引起的断裂。不可聚合的、脑源性或经羧肽酶A处理的骨骼肌原肌球蛋白则不会产生这种保护作用。在F-肌动蛋白丝被原肌球蛋白饱和的条件下,即原肌球蛋白与肌动蛋白的摩尔比为1:7时,F-肌动蛋白会受到针对细胞松弛素和戊二醛作用的保护。有人认为,不可聚合的原肌球蛋白缺乏保护能力,因为它与F-肌动蛋白的结合比可聚合的原肌球蛋白弱得多,并且不能使F-肌动蛋白上的所有结合位点饱和。