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完整枯草芽孢杆菌鞭毛的纯化及热稳定性

Purification and thermal stability of intact Bacillus subtilis flagella.

作者信息

Dimmitt K, Simon M

出版信息

J Bacteriol. 1971 Jan;105(1):369-75. doi: 10.1128/jb.105.1.369-375.1971.

DOI:10.1128/jb.105.1.369-375.1971
PMID:4993323
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC248364/
Abstract

Flagella were prepared and purified in a relatively intact form from bacterial lysates. Immunochemical tests showed that over 95% of the protein in the final preparation consisted of flagellar antigen. These flagella are more stable to thermal denaturation than flagella filaments obtained by shearing. Their thermal properties more closely resemble those of flagella in the native state on bacteria. The presence of the hook structure is responsible for this extra stability.

摘要

鞭毛是从细菌裂解物中以相对完整的形式制备和纯化的。免疫化学测试表明,最终制剂中超过95%的蛋白质由鞭毛抗原组成。这些鞭毛比通过剪切获得的鞭毛丝对热变性更稳定。它们的热性质更类似于细菌中天然状态的鞭毛。钩状结构的存在导致了这种额外的稳定性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8bb8/248364/80a0a94e49b0/jbacter00373-0396-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8bb8/248364/06ee55726816/jbacter00373-0393-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8bb8/248364/80a0a94e49b0/jbacter00373-0396-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8bb8/248364/06ee55726816/jbacter00373-0393-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8bb8/248364/80a0a94e49b0/jbacter00373-0396-a.jpg

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