Abstract
The dynamics of appearance of intracellular proteases in relation to the synthesis of crystal delta-endotoxin was studied to identify the native intracellular protease(s) involved in the proteolytic processing of the 73-kDa protoxin of Bacillus thuringiensis subsp. tenebrionis. In vitro proteolytic activation of the 73-kDa protoxin indicated the possible role of 69-kDa protease in the proteolytic processing of 73-kDa protoxin. The purified 69-kDa protease was able to cause the proteolytic activation of the 73-kDa protoxin to 68-kDa toxin and this conversion was inhibited by ethylenediamine tetraacetic acid and 1,10-phenanthroline.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacillus thuringiensis / enzymology*
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Bacillus thuringiensis / growth & development
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Bacillus thuringiensis / metabolism
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Bacillus thuringiensis Toxins
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Bacterial Proteins / metabolism*
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Bacterial Toxins*
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Electrophoresis, Polyacrylamide Gel
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Endopeptidases / isolation & purification*
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Endopeptidases / metabolism*
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Endotoxins / metabolism*
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Hemolysin Proteins
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Humans
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Immunoblotting
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Metalloendopeptidases / metabolism*
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Protease Inhibitors / pharmacology
Substances
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Bacillus thuringiensis Toxins
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Bacterial Proteins
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Bacterial Toxins
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Endotoxins
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Hemolysin Proteins
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Protease Inhibitors
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insecticidal crystal protein, Bacillus Thuringiensis
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Endopeptidases
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Metalloendopeptidases