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产气荚膜梭菌β-毒素谷胱甘肽S-转移酶融合蛋白的表达与纯化

Expression and purification of Clostridium perfringens beta-toxin glutathione S-transferase fusion protein.

作者信息

Steinthorsdottir V, Fridriksdottir V, Gunnarsson E, Andrésson O S

机构信息

Institute for Experimental Pathology, University of Iceland, Reykjavík.

出版信息

FEMS Microbiol Lett. 1995 Aug 1;130(2-3):273-8. doi: 10.1111/j.1574-6968.1995.tb07731.x.

Abstract

The beta-toxin gene from Clostridium perfringens type C was cloned and expressed as a glutathione S-transferase fusion protein in Escherichia coli. The DNA sequence was determined and compared to the type B sequence. Two nucleotide differences were found in the protein coding sequence, resulting in one amino acid difference between the two proteins. The purified beta-toxin fusion protein is not toxic in mice, but rabbit antiserum raised against it neutralises the toxic effect of C. perfringens type C culture filtrate in mice.

摘要

克隆了产气荚膜梭菌C型的β-毒素基因,并在大肠杆菌中作为谷胱甘肽S-转移酶融合蛋白进行表达。测定了DNA序列并与B型序列进行比较。在蛋白质编码序列中发现了两个核苷酸差异,导致两种蛋白质之间有一个氨基酸差异。纯化的β-毒素融合蛋白对小鼠无毒,但用其制备的兔抗血清可中和产气荚膜梭菌C型培养滤液对小鼠的毒性作用。

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