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Bacterial Expression and Purification of an Active ω-Atracotoxin-Arl b from Spider Atrax robustus
作者单位:[1]Key Laboratory of Plant Protection Resources and Pest Management, Ministry of Education/Northwest A&F University, Yangling 712100 P.R. China [2]College of Forestry, Northwest A&F University, Yangling 712100.P.R.China
基金项目:Acknowledgements This study was supported by the National Natural Science Foundation of China (NSFC-30872033) and the Program for New Century Excellent Talents in University from Ministry of Education, China (NCET-06- 0867).
摘    要:The ω-atracotoxin-Arlb toxin (ω-ACTX-Arl b) is one of the arthropod-selective peptide neurotoxins from the venom of Australian funnel-web spider Atrax robustus. The gene of Arlb was synthesized and cloned into pET-32a(+) vector to allow expression of Arlb as a fusion protein with thioredoxin and the His-tag (rTrx-Arlb) in E. coli BL21 (DE3). The optimal condition for inducing the expression ofrTrx-Arl b was 1.0 mmol L-1 IPTG for 6 h at 28℃. The fusion protein rTrx- Arlb was expressed in soluble form and was purified effectively by HisTrap HP affinity column and rpHLPC and a final yield of purified rTrx-Arlb was 95 mg from 1 000 mL E. coli culture. The LD50 values for Mythimna separate and Tenebrio molitor were 111.66 and 11.04 ug g-1 determined by injection of the purified rTrx-Arlb. The results indicated that the recombinant Arlb protein was successfully expressed in E. coli and it was high toxicity against tested insects.

关 键 词:纯化  蜘蛛  大肠杆菌  细菌  融合蛋白  神经毒素  诱导表达  硫氧还蛋白
收稿时间:1 April 2010
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