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首页> 外文期刊>Journal of bacteriology >Thermoactivation of a periplasmic heat-stable enterotoxin of Escherichia coli.
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Thermoactivation of a periplasmic heat-stable enterotoxin of Escherichia coli.

机译：大肠杆菌的周质热稳定肠毒素的热激活。

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摘要

Strains of Escherichia coli that host a plasmid that codes for the heat-stable (ST) enterotoxin showed 160 times more extracellular enterotoxin than intracellular activity. However, when washed bacteria were sonicated and incubated at between 50 and 85 degrees C, an activity similar to that of the ST enterotoxin was detected. No such effect was present in strains lacking the plasmid, in a plasmid ST- mutant, or in chromosomal mutants that lack a cyclic AMP-linked positive regulatory system which previously were shown to yield an ST- phenotype. The thermoactivation was inhibited by iodoacetamide and N-ethylmaleimide; chloramphenicol did not affect the phenomenon. The heat-activated ST-like enterotoxin was localized in the periplasmic space. The results are discussed in relation to the export of the toxin from the periplasm to the outside of the cell.
机译：带有编码热稳定（ST）肠毒素编码质粒的大肠杆菌菌株显示的细胞外肠毒素比细胞内活性高160倍。然而，当将洗涤过的细菌超声处理并在50至85摄氏度之间孵育时，检测到的活性与ST肠毒素相似。在缺少质粒的菌株中，在质粒ST突变体中或在缺乏环状AMP连接的正调控系统的染色体突变体中均没有这种作用，先前已证明它们产生ST表型。碘乙酰胺和N-乙基马来酰亚胺抑制了热活化。氯霉素没有影响该现象。热活化的ST样肠毒素位于周质空间。讨论了有关毒素从周质向细胞外部输出的结果。

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