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Mol Cell Biochem. 1995 Apr 12;145(1):29-37.

A glycoprotein multimer from Bacillus thuringiensis sporangia: dissociation into subunits and sugar composition.

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Instituto de Investigaciones Bioquímicas, Fundación Campomar, Buenos Aires, Argentina.


Two glycoproteins (205 and 72 kDa) were found in Bacillus thuringiensis sporangia. They were predominantly localized in the exosporium and/or the spore coat, although a small proportion was also found in membranes. A method for the dissociation of hydrophobic aggregates that resist the usual conditions of SDS-PAGE is described. Using this method we established that the 205 kDa glycoprotein is a multimer of the 72 kDa one. Deglycosylation of the 205 kDa and 72 kDa glycoproteins with trifluoromethanesulfonic acid yielded a 54 kDa polypeptide in both cases. At least three species of oligosaccharides were O-glycosidically linked to serines of the 54 kDa polypeptide chain. One of the oligosaccharides had N-acetylgalactosamine at the reducing end, rhamnose and a component not yet identified.

[Indexed for MEDLINE]

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