苏云金芽孢杆菌以色列亚种毒素被释放到培养基中的蚊虫幼虫蛋白酶灭活。
The inactivation of Bacillus thuringiensis subsp. israelensis toxin by mosquito larvae proteases liberated into the medium.
作者信息
García-Patrone M, Reboredo R G, Torres H N, Rubinstein C, Stoka A
出版信息
Biochem Biophys Res Commun. 1986 Mar 28;135(3):902-8. doi: 10.1016/0006-291x(86)91013-2.
Crystal serine-proteases of B. thuringiensis subsp. israelensis were able to process the 28,000-dalton protein during crystal solubilization. On the other hand, solubilized crystal proteins were degraded during the larvicidal bioassay by the action of serine-proteases liberated by mosquito larvae into the medium, with loss of toxicity. However, proteins in intact crystals were protected from the action of these proteases. This resistance to degradation of crystals partly explains the observation that they are more toxic than solubilized crystal proteins.
苏云金芽孢杆菌以色列亚种的晶体丝氨酸蛋白酶能够在晶体溶解过程中加工28,000道尔顿的蛋白质。另一方面，在杀幼虫生物测定过程中，溶解的晶体蛋白会被蚊子幼虫释放到培养基中的丝氨酸蛋白酶降解，从而失去毒性。然而，完整晶体中的蛋白质受到这些蛋白酶作用的保护。晶体对降解的这种抗性部分解释了它们比溶解的晶体蛋白毒性更强这一现象。
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