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- W179430170 abstract "Tryptic digestion of the proteins from the purified crystals of B. thuringiensis var israelensis resulted in the decline of high molecular weight peptides without the loss of mosquito larvicidal activity, measured after immobilization of the digests with DEAE- Sephadex A 50 beads. Amongst the peptides generated (<44 kDa), a 21 kDa peptide was immunoreactive to the crystal antiserum. Analysis of the peptides released from spores of the toxic (Cry+) and non-toxic (Cry−) strains has revealed a pattern in which only the 26kDa peptide was missing in the Cry-strain. Sporulation and crystal formation were dissociated by the addition of the antibiotic netropsin, which could also inhibit the crystal assembly, without considerable decrease of the larvicidal activity and retention of the 26kDa peptide. These results implicate the 26kDa peptide in the larvicidal action." @default.
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- W179430170 date "1985-10-01" @default.
- W179430170 modified "2023-09-24" @default.
- W179430170 title "Identification of the peptides of the crystals of Bacillusthuringiensis var israelensis involved in the mosquito larvicidal activity" @default.
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- W179430170 doi "https://doi.org/10.1016/0006-291x(85)90982-9" @default.
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