Effect of Removal of the Cytolytic Factor of 'Bacillus thuringiensis' Subsp. 'Israelensis' on Mosquito Toxicity

摘要

Solubilized crystal protein of Bacillus thuringiensis subsp. israelensis was fractionated by affinity chromotography using a monoclonal antibody directed against the crystal's 28 kDa peptide. The 28 kDa peptide ws found to be relatively nontoxic to mosquito larvae although it does contain the hemolytic activity of the crystals. The crystal protein fraction depleted of the 29 kDa peptide was found to be nonhemolytic and to retain nearly full toxicity to mosquito larvae. These results suggest that the 28 kDa peptide is not required for the toxicity of solubilized crystal protein.