[Proteins and proteinase-resistant polypeptides of delta-endotoxins from Bacillus thuringiensis and their insecticidal activity].

Proteins, solubility in alkaline buffer and proteinase-resistant polypeptides (PRP) of parasporal crystals (delta-endotoxin) from Bacillus thuringiensis were investigated. 19 sorts of crystals were divided into 7 types. Difference of crystalline proteins were coincident with their solubility and PRP. The characters of the protein, solubility and PRP were subspecies-specific basically, but in a few of crystals they were strain-specific. There was a closed relation between the biochemistry property of crystal protein and the toxicity in 2 species of insects. Crystal with protein of MW 130-138 kD kD or MW 130-138 kD and 60-65 kD, and PRP of MW 68-75 kD were high toxic in Bombyx mori (Lepidoptera), but most of them only showed weak or no toxicity in Culex fatigans (Diptera). Crystals containing more than 3 sorts of proteins with MW 15-138 kD in major protein and MW 35-75 kD in minor protein and PRP of 35-65 kD had very strong toxicity in Culex fatigans, but no toxicity in Bombyx mori. The construct of the crystal protein and the importance of the character in protein and PRP for the selection of expected strain and for the work of genetic engineering in Bacillus thuringiensis were discussed.