An electron microscope study of the interaction between fructose diphosphate aldolase and actin-containing filaments
An electron microscope study of the interaction between fructose diphosphate aldolase and actin-containing filaments
复制标题
果糖二磷酸醛缩酶与含肌动蛋白丝之间相互作用的电子显微镜研究
作者：
D. Morton;F. Clarke;C. Masters
用负染法研究了果糖二磷酸醛缩酶与F-肌动蛋白、F-肌动蛋白-原肌球蛋白和F-肌动蛋白-原肌球蛋白-肌钙蛋白的相互作用。在缺乏肌钙蛋白的情况下，会形成醛缩酶和F-肌动蛋白丝的微小聚集体。只有在完全重构的丝的情况下，当纳米纤维与丝的间距为18 nm，并且跨桥间距为38.7nm时，才形成良好有序的晶格结构。证据表明，晶格是由于肌钙蛋白和醛缩酶之间的相互作用。肌钙蛋白的最小亚基结构仍然能够产生晶格，是肌钙蛋白-IT复合物，这表明肌钙蛋白-C不参与醛缩酶结合。
The interaction of fructose diphosphate aldolase with F-actin, F-actin- tropomyosin, and F-actin-tropomyosin-troponin has been studied by using negative staining. In the absence of troponin, minor aggregates of aldolase and the F-actin filaments are formed. A well-ordered lattice structure is only formed in the case of the fully reconstituted filament when the filament-to-filament spacing is 18nm, and the cross- bridge spacing is 38.7 nm. Evidence is presented that the lattice is due to an interaction between troponin and aldolase. The minimum subunit structure of troponin, still capable of giving rise to a lattice, is the troponin-IT complex, which indicates that troponin-C is not involved in aldolase binding.