Comparative analysis of proteinase activities of Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis (Lepidoptera: Crambidae)
Comparative analysis of proteinase activities of Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis (Lepidoptera: Crambidae)
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DOI：
10.1016/j.ibmb.2004.03.010
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发表时间：
2004-08-01
影响因子：
3.8
通讯作者：
Buschman, LL
中科院分区：
文献类型：
--
作者：
Li, HR;Oppert, B;Buschman, LL
比较了抗苏云金杆菌和感苏云金杆菌玉米螟幼虫肠道可溶性组分和膜组分的蛋白酶活性。总的来说，从敏感菌株的可溶性组分的丝氨酸蛋白酶比那些抗性菌株更活跃。抗性菌株的可溶性胰蛋白酶样蛋白酶活性约为敏感菌株的一半。可溶性和膜性丝氨酸蛋白酶的数量和相对分子质量不同。然而，有两个菌株的中肠膜提取的丝氨酸蛋白酶和氨基肽酶的活性没有显着差异。抗性菌株的可溶性蛋白酶提取物对Cry 1Ab原毒素的水解相对于敏感菌株降低约20-30%。由于Bt原毒素活化蛋白酶活性降低，导致原毒素加工减少，这可能与该抗性株对Bt毒素的抗性有关。nubilalis (C)2004 Elsevier Ltd.保留所有权利。
Proteinase activities were compared in soluble and membrane fractions of guts obtained from larvae of Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis. Overall, serine proteinases from soluble fractions of the susceptible strain were more active than those of the resistant strain. The soluble trypsin-like proteinase activity of the resistant strain was approximately half that of the susceptible strain. The number and relative molecular masses of soluble and membrane serine proteinases were different. However, there were no significant differences in the activities of serine proteinases and aminopeptidases extracted from midgut membranes of the two strains. Cry1Ab protoxin hydrolysis by soluble proteinase extracts of the resistant strain was reduced approximately 20-30% relative to that of the susceptible strain. Reduced protoxin processing due to decreased activities of Bt protoxin activation proteinases may be associated with resistance to Bt toxin in this resistant strain of O. nubilalis. (C) 2004 Elsevier Ltd. All rights reserved.