Purification and characterization of a polyhook protein from Caulobacter crescentus
Purification and characterization of a polyhook protein from Caulobacter crescentus
复制标题
新月柄杆菌多钩蛋白的纯化和表征
DOI：
10.1128/jb.138.2.575-583.1979
复制
发表时间：
1979
影响因子：
3.2
通讯作者：
A. Newton
中科院分区：
文献类型：
--
作者：
M. Sheffery;A. Newton
分离到一株多钩产生菌，并对其多钩蛋白进行了纯化。多钩结构的抗原性和形态与野生型钩相似，不同的是突变株产生的钩状结构至少是野生型钩子长度的10倍(1.0微米对0.1微米)。经十二烷基硫酸钠-聚丙烯酰胺凝胶电泳法测定，该多钩蛋白的相对分子质量为72,000，等电点约为6.1。针对该多钩蛋白制备的抗体被用来证明该蛋白在抗原性上不同于Caulbacter鞭毛蛋白。多钩蛋白的氨基酸分析显示，其组成与其他革兰氏阴性细菌钩蛋白相似。
A polyhook-producing strain of Caulobacter crescentus was isolated, and the polyhook protein was purified. The antigenicity and morphology of the polyhook structure are similar to the wild-type hook except that the mutant strain produces a hook structure at least 10-fold the length of wild-type hooks (1.0 versus 0.1 micrometers). The molecular weight of the polyhook protein, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, is 72,000, and the protein has a pI of approximately 6.1. Antibodies prepared against the polyhook protein were used to show that this protein is antigenically distinct from the Caulobacter flagellins. Amino acid analysis of the polyhook protein revealed compositional similarities to other gram-negative, bacterial hook proteins.