Glenney J R, Glenney P, Weber K
J Biol Chem. 1982 Aug 25;257(16):9781-7.
The axonally transported high molecular weight protein fodrin, known to be present in the cortical cytoplasm of neurones and other cells, has been purified to homogeneity and several of its biochemical properties have been characterized. Fodrin is an F-actin-binding and cross-linking protein inducing actin gels. It is composed of two nonidentical polypeptide chains (Mr = 240,000 and 235,000) which form a tetrameric complex of a molecular weight close to 930,000. The similarity of fodrin with tetrameric erythrocyte spectrin is directly shown by rotary shadowed molecules both alone and in interaction with F-actin. The gelation and cross-linking activity of fodrin is influenced both by ionic strength and pH in a manner similar to other cross-linking factors. These results strengthen previous concepts concerning the existence of spectrin-related molecules in nonerythroid cells and point to a possible related function in the submembranous microfilament organization in nonmuscle cells.
轴突运输的高分子量蛋白血影蛋白，已知存在于神经元和其他细胞的皮质细胞质中，已被纯化至同质，并对其一些生化特性进行了表征。血影蛋白是一种F-肌动蛋白结合和交联蛋白，可诱导肌动蛋白凝胶形成。它由两条不同的多肽链（Mr = 240,000和235,000）组成，形成分子量接近930,000的四聚体复合物。单独的旋转阴影分子以及与F-肌动蛋白相互作用的旋转阴影分子直接显示了血影蛋白与四聚体红细胞血影蛋白的相似性。血影蛋白的凝胶化和交联活性受离子强度和pH的影响，其方式与其他交联因子相似。这些结果强化了先前关于非红细胞中存在血影蛋白相关分子的概念，并指出了在非肌肉细胞的膜下微丝组织中可能存在的相关功能。
