从四膜虫纤毛中获得的14S动力蛋白的结构和质量分析
Structure and mass analysis of 14S dynein obtained from Tetrahymena cilia.
作者信息
Marchese-Ragona S P, Wall J S, Johnson K A
机构信息
Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.
出版信息
J Cell Biol. 1988 Jan;106(1):127-32. doi: 10.1083/jcb.106.1.127.
Abstract
Scanning transmission electron microscopic analysis revealed that the 14S fraction of Tetrahymena dynein was of a mixture of two types of particles in approximately equal proportions. The 14S dynein molecules were roughly ellipsoid in shape with approximate axes of 9.5 and 14.5 nm. About half of the particles had tails 20-24-nm long. By the integration of electron scattering intensities, particles with tails had an average mass of 510 kD with a SD of 90 kD. The globular heads of both types of particles had an average mass of 330 kD with a SD of 60 kD. The mass of the tail structure was about 180 kD. By SDS-PAGE, the 14S dynein consisted of two high molecular mass polypeptides above 300 kD that could be distinguished by immunoblot analysis.
摘要
扫描透射电子显微镜分析显示，四膜虫动力蛋白的14S组分是两种类型颗粒的混合物，比例大致相等。14S动力蛋白分子大致呈椭圆形，长轴约9.5纳米，短轴约14.5纳米。约一半的颗粒有20 - 24纳米长的尾部。通过电子散射强度积分，有尾部的颗粒平均质量为510千道尔顿，标准差为90千道尔顿。两种类型颗粒的球状头部平均质量为330千道尔顿，标准差为60千道尔顿。尾部结构的质量约为180千道尔顿。通过十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳（SDS - PAGE）分析，14S动力蛋白由两条分子量高于300千道尔顿的高分子量多肽组成，这两条多肽可通过免疫印迹分析加以区分。
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