Abstract
Protein profiles of crystal delta-endotoxins were determined in twenty nine Bacillus thuringiensis strains-soil and phylloplane isolates--from Poland. Electrophoretic analysis revealed quantatively and qualitatively different patterns of delta-endotoxin crystal preparations of these B. thuringiensis strains. The crystalline parasporal inclusions of B. thuringiensis isolates were composed of two, three, four or five proteins. Molecular weights of these polypeptides varied from 23.4 kDa to 142 kDa. There is lack of correlation between serovars of B. thuringiensis strains, the morphology of crystals and the number and size of proteins in parasporal inclusions.
MeSH terms
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Bacillus thuringiensis / chemistry*
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Bacillus thuringiensis / classification
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Bacillus thuringiensis / isolation & purification*
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Bacillus thuringiensis Toxins
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Bacterial Proteins / chemistry*
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Bacterial Proteins / isolation & purification
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Bacterial Toxins / chemistry*
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Bacterial Toxins / isolation & purification
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Crystallization
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Electrophoresis, Polyacrylamide Gel
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Endotoxins / chemistry*
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Endotoxins / isolation & purification
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Hemolysin Proteins
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Inclusion Bodies / chemistry
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Molecular Weight
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Poland
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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insecticidal crystal protein, Bacillus Thuringiensis