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新月柄杆菌多钩蛋白的纯化与特性分析

Purification and characterization of a polyhook protein from Caulobacter crescentus.

作者信息

Sheffery M, Newton A

出版信息

J Bacteriol. 1979 May;138(2):575-83. doi: 10.1128/jb.138.2.575-583.1979.

Abstract

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.

摘要

分离出了一株能产生多钩的新月柄杆菌菌株,并对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,只是突变菌株产生的钩结构长度至少是野生型钩的10倍(1.0微米对0.1微米)。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定,多钩蛋白的分子量为72,000,该蛋白的pI约为6.1。针对多钩蛋白制备的抗体表明,这种蛋白在抗原性上与柄杆菌鞭毛蛋白不同。对多钩蛋白的氨基酸分析显示,其组成与其他革兰氏阴性菌的钩蛋白相似。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4880/218215/e2190e7877ce/jbacter00282-0297-a.jpg

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