Clarke F M, Morton D J
Biochem J. 1976 Dec 1;159(3):797-8. doi: 10.1042/bj1590797.
Electron-microscopy observation show that when aldolase binds to F-actin or F-actin-tropomyosin, highly ordered paracrystalline structures are formed consisting of tightly packed filament bundles cross-banded at 36 nm intervals. Morphologically different paracrystalline arrays are formed between aldolase and F-actin-tropomyosin-troponin. The filament bundles are far more extensive and are characterized by a prominent cross-striation at 38nm intervals. It is suggested that this reflects an interaction between troponin and aldolase.
电子显微镜观察显示,当醛缩酶与F-肌动蛋白或F-肌动蛋白-原肌球蛋白结合时,会形成高度有序的类晶体结构,该结构由紧密排列的细丝束组成,这些细丝束以36纳米的间隔交叉带纹。醛缩酶与F-肌动蛋白-原肌球蛋白-肌钙蛋白之间形成了形态不同的类晶体阵列。细丝束更为广泛,其特征是有明显的38纳米间隔的交叉条纹。这表明这反映了肌钙蛋白与醛缩酶之间的相互作用。