The toxicity of twoBacillus thuringiensis δ-endotoxins to gypsy moth larvae is inversely related to the affinity of binding sites on midgut brush border membranes for the toxins

@article{Wolfersberger1990TheTO,
  title={The toxicity of twoBacillus thuringiensis δ-endotoxins to gypsy moth larvae is inversely related to the affinity of binding sites on midgut brush border membranes for the toxins},
  author={M. G. Wolfersberger},
  journal={Experientia},
  year={1990},
  volume={46},
  pages={475-477}
}
Theδ-endotoxin fromBacillus thuringiensis subspecieskurstaki strain HD1-9 is almost 400 times more potent than theδ-endotoxin from strain HD-73 as a gypsy moth larvicide. The twoδ-endotoxins compete for a high-affinity binding site on the brush border membrane of larval gypsy moth midguts. The affinity for theδ-endotoxin from strain HD-73 is much greater than the affinity for theδ-endotoxin from strain HD1-9. 

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