Abstract
Delta-endotoxins from three new strains of Bacillus thuringiensis were purified using DEAE-Sephadex column chro-matography. Proteolytic cleavage of the purified delta-endotoxins, using trypsin and chymotrypsin, gave different polypeptide patterns predicting differences in their aminoacids sequences. These differences were confirmed by a detailed immunological study, which revealed that the delta-endotoxins exhibit a degree of 30% to 40% homology.
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