SUMMARY: Entomocidal proteins produced by certain subspecies of were isolated from purified crystals (parasporal bodies) by column chromatography using Sephacryl S-300. The crystals of most subspecies contained only one entomocidal protein (P-1), but some strains of which had been classified as subsp. , subsp. , subsp. and subsp. appeared to produce an additional protein (P-2) as a minor component of the crystal. The protein (P-2) was serologically similar to the mosquito factor previously discovered in the HD-1 strain of subsp. These entomocidal proteins (P-and P-2) were isolated and digested by trypsin. The peptides resulting from the trypsin digestion were mapped by high performance liquid chromatography (HPLC). HPLC patterns of the toxins, in particular P-1, were reliably reproducible and revealed differences in P-1 toxins between strains even in the same serotype. Analysis of P-2 by HPLC indicated that it is different from P-1 in protein structure.


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