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首页> 外文期刊>Journal of bacteriology >In vitro binding of cloacin DF13 to its purified outer membrane receptor protein and effect of peptidoglycan on bacteriocin-receptor interaction.
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In vitro binding of cloacin DF13 to its purified outer membrane receptor protein and effect of peptidoglycan on bacteriocin-receptor interaction.

机译:cloacin DF13与其体外纯化的外膜受体蛋白的体外结合以及肽聚糖对细菌素-受体相互作用的影响。

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摘要

The in vitro neutralization of the killing activity of cloacin DF13 by incubation with its purified receptor protein was shown to be the result of the formation of a direct and specific equimolar complex of both proteins. The binding of cloacin DF13 to its receptor protein did not result in a fragmentation of the cloacin molecules nor in the expulsion of immunity protein from the bacteriocin. The rate of the cloacin DF13-receptor interaction in vitro was found to be enhanced significantly in the presence of peptidoglycan, but lysozyme-treated peptidoglycan did not affect this interaction. Incubation of the cloacin DF13 as well as its receptor protein with peptidoglycan showed that the receptor protein but not the cloacin DF13 was able to bind to the peptidoglycan.
机译:通过与氯丁香DF13的纯化受体蛋白孵育,体外中和泄殖腔DF13的杀伤活性被证明是两种蛋白直接和特异性等摩尔复合物形成的结果。 cloacin DF13与其受体蛋白的结合不会导致cloacin分子断裂,也不会导致免疫蛋白从细菌素中排出。发现在存在肽聚糖的情况下,cloacin DF13-受体相互作用的速率在体外显着提高,但是溶菌酶处理的肽聚糖不影响这种相互作用。将cloacin DF13及其受体蛋白与肽聚糖一起孵育表明,受体蛋白而非cloacin DF13能够与肽聚糖结合。

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