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• W2003247236 startingPage "70" @default.
• W2003247236 abstract "Toxicity tests were performed to find among Cry1 and Cry2 Bacillus thuringiensis crystal proteins those with high activity against the cabbage looper. Tests were performed with neonate larvae on surface-contaminated artificial diet. The crystal proteins found to be toxic were, from higher to lower toxicity: Cry1Ac, Cry1Ab, Cry1C, Cry2Aa, Cry1J, and Cry1F (LC50 of 1.14.1, 3.4-4.4, 12, 34, 87, and 250 ng/cm2, respectively). Cry1B, Cry1D, and Cry1E can be considered nontoxic (LC50 higher than 2500 ng/cm2). Cry1Aa was moderately toxic to nontoxic, depending on the source (LC50 of 420 ng/cm2 from PGS and 8100 ng/cm2 from Ecogen). In vitro binding assays with trypsin-activated 125I-labeled Cry1Aa, Cry1Ab, and Cry1Ac crystal proteins and brush border membrane vesicles from midgut larvae showed a direct correlation between toxicity and binding affinity. Heterologous competition experiments indicated that Cry1Aa and Cry1F bind, though only at very high concentrations, to the Cry1Ab/Cry1Ac shared high-affinity binding site." @default.
• W2003247236 created "2016-06-24" @default.
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• W2003247236 date "2000-07-01" @default.
• W2003247236 modified "2023-10-16" @default.
• W2003247236 title "Screening for Bacillus thuringiensis Crystal Proteins Active against the Cabbage Looper, Trichoplusia ni" @default.
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• W2003247236 doi "https://doi.org/10.1006/jipa.2000.4946" @default.
• W2003247236 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10963406" @default.
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