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首页> 外文期刊>Infection and immunity >Adenylate cyclase toxin of Bordetella pertussis: production, purification, and partial characterization.
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Adenylate cyclase toxin of Bordetella pertussis: production, purification, and partial characterization.

机译：百日咳博德特氏菌的腺苷酸环化酶毒素：生产，纯化和部分表征。

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摘要

Bordetella pertussis produces a number of virulence determinants which contribute to its pathogenicity. One factor, the adenylate cyclase toxin (ACT), has been suggested to directly penetrate human phagocytes and disrupt their normal function by direct production of intracellular cyclic AMP (cAMP). Experiments evaluating the production of cell-associated ACT in liquid cultures of B. pertussis 504 demonstrated that the greatest activity was observed during mid-log-phase growth. Urea extracts of cells harvested during the time of maximal ACT production have been used to purify the toxin with both biological and enzymatic activities. ACT is a protein with an apparent molecular mass of 220 kDa and an isoelectric point of 7.0. The specific activity of purified ACT is 17,000 mumol of cAMP formed per mg per min. The the biological specific activity of purified ACT is 6,250 nmol of intracellular cAMP formed per mg per min in 2 x 10(6) S49 lymphoma cells per ml. Preparations containing 8 micrograms of ACT completely abrogated the chemiluminescence response of 2 x 10(6) human neutrophils per ml.
机译：百日咳博德特氏菌产生许多致病因素，导致其致病性。已建议一种因素，腺苷酸环化酶毒素（ACT）直接穿透人吞噬细胞，并通过直接产生细胞内环AMP（cAMP）破坏其正常功能。评估百日咳百日咳杆菌504液体培养物中细胞相关ACT产生的实验表明，在对数中期生长期间观察到最大的活性。在最大的ACT产生期间收获的细胞尿素提取物已用于纯化具有生物学和酶促活性的毒素。 ACT是一种蛋白质，其表观分子量为220 kDa，等电点为7.0。纯化的ACT的比活性为每毫克每分钟17,000摩尔cAMP。在每毫升2 x 10（6）S49淋巴瘤细胞中，纯化的ACT的生物比活性是每毫克每分钟形成6,250 nmol的细胞内cAMP。包含8微克ACT的制剂完全消除了每毫升2 x 10（6）个人嗜中性粒细胞的化学发光反应。

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