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首页> 外文期刊>Infection and immunity >Proteolysis of Clostridium perfringens type A enterotoxin during purification.
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Proteolysis of Clostridium perfringens type A enterotoxin during purification.

机译：纯化过程中产气荚膜梭状芽孢杆菌肠毒素的蛋白水解。

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The small satellite bands of enterotoxin frequently seen in polyacrylamide gels following purification of Clostridium perfringens enterotoxin were found to be due to endogenous protease activity and were not present if phenylmethylsulfonyl fluoride (PMSF; 1 mM) and EDTA (10 mM) were used in the purification protocol. The use of PMSF was avoided by passing gel filtration-purified enterotoxin material through DEAE-Sephacel. This modified protocol resulted in an 11.4-fold purification of enterotoxin and a 26.8% yield. Contrary to previous reports (B. R. Dasgupta and M. W. Pariza, Infect. Immun. 38: 592-597, 1982), if PMSF and EDTA were included during purification, we were unable to detect the novel enterotoxin ET-1 produced by strain NCTC 10240. C. perfringens proteases cleaved homogeneous enterotoxin into two additional fragments, suggesting that ET-1 was a product of endogenous protease action during purification.
机译：纯化产气荚膜梭菌肠毒素后在聚丙烯酰胺凝胶中经常见到的肠毒素小卫星带是由于内源蛋白酶活性引起的，如果在纯化中使用苯甲基磺酰氟（PMSF; 1 mM）和EDTA（10 mM）则不存在协议。通过使凝胶过滤纯化的肠毒素材料通过DEAE-Sephacel，避免了PMSF的使用。修改后的方案可导致肠毒素的11.4倍纯化和26.8％的产率。与以前的报道（BR Dasgupta和MW Pariza，Infect。Immun。38：592-597，1982）相反，如果在纯化过程中包括PMSF和EDTA，我们将无法检测到NCTC 10240菌株产生的新型肠毒素ET-1。产气荚膜梭菌蛋白酶将均质肠毒素切割成两个另外的片段，表明ET-1是纯化过程中内源蛋白酶作用的产物。

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