Affinity purification of a 65-kilodalton parasporal protein from Bacillus thuringiensis PG-14 that shows mosquitocidal activity.
By using antibody-mediated affinity chromatography, a highly mosquito larvicidal but nonhemolytic fraction was obtained from alkali-solubilized, silkworm (Bombyx mori) larval gut juice-treated parasporal inclusions of Bacillus thuringiensis strain PG-14 (serotype 8a:8b). This fraction contained a 65-kDa protein only but not a 25-kDa protein, the main component in the flow through fraction unbound to the affinity column. The 25-kDa protein purified from the unbound fraction by CM-cellulose chromatography demonstrated a high hemolytic activity against sheep red blood cells but very low mosquito larvicidal activity.
Institute of Biological Control, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
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YM
Yu
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Ohba
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Aizawa
D000330:Aedes; D000818:Animals; D000942:Antigens, Bacterial / Q000302:isolation & purification; D001413:Bacillus thuringiensis / Q000032:analysis*; D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006460:Hemolysin Proteins; D007306:Insecticides / Q000302:isolation & purification*; D007814:Larva; D007928:Lethal Dose 50; D008970:Molecular Weight; D012756:Sheep; D013171:Spores, Bacterial / Q000032:analysis
D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D006460:Hemolysin Proteins; D007306:Insecticides