Proteolytic processing of the mosquitocidal toxin from Bacillus sphaericus SSII-1.

@article{Thanabalu1992ProteolyticPO,
  title={Proteolytic processing of the mosquitocidal toxin from Bacillus sphaericus SSII-1.},
  author={Thirumaran Thanabalu and J. Hindley and Colin Berry},
  journal={Journal of bacteriology},
  year={1992},
  volume={174 15},
  pages={5051-6}
}
The 97-kDa protein Mtx21, derived from the 100-kDa mosquitocidal protein (Mtx) from Bacillus sphaericus SSII-1 by the deletion of the putative signal sequence, was expressed as a fusion protein with glutathione S-transferase in Escherichia coli, and the fusion protein was purified by affinity chromatography. The fusion protein bound to glutathione agarose was cleaved with thrombin to release the Mtx21 protein. The 97-kDa Mtx21 protein was found to be toxic to Culex quinquefasciatus larvae with… CONTINUE READING
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Another Bacillus serotype harbouring strains very toxic to mosquito larvae: serotype H6

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quence analysis of the mosquitocidal toxin genes encoding 51 . 4 - and 41 . 9 - kilodalton proteins from Bacillus sphaencus 2362 and 2297

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