网格蛋白轻链的原肌球蛋白样特性可实现快速、高产率的纯化。
Tropomyosin-like properties of clathrin light chains allow a rapid, high-yield purification.
作者信息
Brodsky F M, Holmes N J, Parham P
出版信息
J Cell Biol. 1983 Mar;96(3):911-4. doi: 10.1083/jcb.96.3.911.
Abstract
The light chains (LCa and LCb) of bovine brain clathrin are resistant to heat denaturation by boiling, a property shared by tropomyosin (Bailey, K., 1948, Biochem. J., 43:271-281). Light chains were partially purified by boiling and centrifugation of a Tris-extract of crude membranes prepared from bovine brains (Keen, J. H., M. C. Willingham, and I. H. Pastan, 1979, Cell., 16:303-312). Contaminant polypeptides were then removed by size-exclusion high-pressure liquid chromatography. The purified light chains were separated from each other by using an immunoaffinity column prepared from a monoclonal antibody CVC.7 specific for LCa and not LCb.
摘要
牛脑网格蛋白的轻链（LCa和LCb）对煮沸引起的热变性具有抗性，原肌球蛋白也具有这一特性（贝利，K.，1948年，《生物化学杂志》，43:271 - 281）。通过对牛脑制备的粗膜Tris提取物进行煮沸和离心，对轻链进行了部分纯化（基恩，J. H.，M. C. 韦林厄姆，和I. H. 帕斯坦，1979年，《细胞》，16:303 - 312）。然后通过尺寸排阻高压液相色谱法去除污染性多肽。使用由对LCa而非LCb具有特异性的单克隆抗体CVC.7制备的免疫亲和柱，将纯化的轻链彼此分离。
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