Characterization of the entomocidal parasporal crystal of Bacillus thuringiensis.
作者： L A Bulla , K J Kramer , L I Davidson
DOI: 10.1128/JB.130.1.375-383.1977
关键词:
摘要: The parasporal crystalline protoxin of Bacillus thuringiensis contains a single glycoprotein subunit that has molecular weight approximately 1.2 X 10(5). carbohydrate consists glucose (3.8%) and mannose (1.8%). At alkaline pH, the proendotoxin is apparently solubilized activated by an autolytic mechanism involving inherent sulfhydryl protease renders insecticidal. Activation generates protons, degraded polypeptides, group reactivity, proteolytic activity, insect toxicity. Chemical modification groups inhibits insecticidal activities, suggesting cysteine residues may be present in active site protein.
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