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
- 1 May 1990
- journal article
- research article
- Published by Springer Nature in Cellular and Molecular Life Sciences
- Vol. 46 (5), 475-477
- https://doi.org/10.1007/bf01954236
Abstract
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.Keywords
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