内源性酶对B型肉毒梭菌毒素的激活作用。
Activation of Clostridium botulinum type B toxin by an endogenous enzyme.
作者信息
DasGupta B R
出版信息
J Bacteriol. 1971 Dec;108(3):1051-7. doi: 10.1128/jb.108.3.1051-1057.1971.
Abstract
It was previously postulated, based on indirect evidence, that Clostridium botulinum type B produces neurotoxin which is initially of low toxicity but which then becomes activated to highly toxic form by the action of an endogenous enzyme(s). The first direct in vitro experimental evidence in support of this hypothesis is presented here. The mildly active toxin (progenitor toxin) produced by C. botulinum type B (Lamanna) was isolated from the filtrate of a 24-hr culture and partially purified chromatographically. An enzyme that activates the progenitor toxin was also isolated from the filtrate of a 96-hr culture and purified 200-fold. The enzyme hydrolyzes synthetic substrates of trypsin but not of chymotrypsin.
摘要
此前基于间接证据推测，B型肉毒梭菌产生的神经毒素最初毒性较低，但随后通过一种内源性酶的作用被激活为高毒性形式。本文提供了支持这一假说的首个直接体外实验证据。从24小时培养物的滤液中分离出B型肉毒梭菌（拉曼纳氏菌）产生的活性较弱的毒素（前体毒素），并通过色谱法进行部分纯化。还从96小时培养物的滤液中分离出一种激活前体毒素的酶，并将其纯化了200倍。该酶能水解胰蛋白酶的合成底物，但不能水解糜蛋白酶的合成底物。
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