Differentiated pattern of protein composition of crystalline inclusions of newly isolated Bacillus thuringiensis strains from Silesia in Poland.

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.