Pachter J S, Liem R K
J Cell Biol. 1985 Oct;101(4):1316-22. doi: 10.1083/jcb.101.4.1316.
In this paper we describe a 66-kD protein that co-purifies with intermediate filaments from rat optic nerve and spinal cord but can be separated further by ion-exchange chromatography. This protein is distinct from the 68-kD neurofilament subunit protein as judged by isoelectric focusing, immunoblotting, peptide mapping, and tests of polymerization competence. This protein is avidly recognized by the monoclonal anti-intermediate filament antigen antibody, previously demonstrated to recognize a common antigenic determinant in all five known classes of intermediate filaments. Also, when isolated this protein binds to various intermediate filament subunit proteins, which suggests an in vivo interaction with the intermediate filament cytoskeleton, and it appears to be axonally transported in the rat optic nerve. Because of this ability to bind to intermediate filaments in situ and in vitro we have named this protein alpha-internexin. A possible functional role for the protein in organizing filament assembly and distribution is discussed.
在本文中,我们描述了一种66-kD蛋白,它与大鼠视神经和脊髓中的中间丝共同纯化,但可通过离子交换色谱进一步分离。通过等电聚焦、免疫印迹、肽图谱分析和聚合能力测试判断,该蛋白与68-kD神经丝亚基蛋白不同。该蛋白被单克隆抗中间丝抗原抗体强烈识别,先前已证明该抗体可识别所有已知的五类中间丝中的共同抗原决定簇。此外,该蛋白分离后可与各种中间丝亚基蛋白结合,这表明它在体内与中间丝细胞骨架相互作用,并且在大鼠视神经中似乎是轴突运输的。由于该蛋白在原位和体外均具有与中间丝结合的能力,我们将其命名为α-间连蛋白。本文还讨论了该蛋白在组织丝组装和分布中的可能功能作用。