结蛋白原丝的结构特征。

Structural characteristics of the desmin protofilament.

作者信息

Milam L, Erickson H P

出版信息

J Ultrastruct Res. 1984 Nov;89(2):179-86. doi: 10.1016/s0022-5320(84)80013-1.

Abstract

Biochemical investigations of intermediate filaments in soluble or partially assembled forms are often difficult to perform due to the unusual insolubility of most types of intermediate filaments. However, desmin is soluble in 10 mM Tris. The structure of partially soluble native desmin was studied by gel-filtration chromatography and electron microscopy. The lowest molecular weight species of soluble desmin is a flexible rod averaging 53 nm in length. Calculations of f/fmin values from a previously published sedimentation value allowed comparisons with other elongated proteins. These values and the dimensions obtained from electron microscopy suggest that the desmin protofilament contains three or four protein subunits.

摘要

由于大多数类型的中间丝具有不同寻常的不溶性，对可溶性或部分组装形式的中间丝进行生化研究往往很难开展。然而，结蛋白可溶于10 mM Tris中。通过凝胶过滤色谱法和电子显微镜对部分可溶的天然结蛋白的结构进行了研究。可溶性结蛋白的最低分子量种类是一种平均长度为53 nm的柔性杆状物。根据先前发表的沉降值计算f/fmin值，以便与其他细长蛋白质进行比较。这些值以及从电子显微镜获得的尺寸表明，结蛋白原丝包含三个或四个蛋白质亚基。