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A glycoprotein multimer fromBacillus thuringiensis sporangia: Dissociation into subunits and sugar composition

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Abstract

Two glycoproteins (205 and 72 kDa) were found inBacillus 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.

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García-Patrone, M., Tandecarz, J.S. A glycoprotein multimer fromBacillus thuringiensis sporangia: Dissociation into subunits and sugar composition. Mol Cell Biochem 145, 29–37 (1995). https://doi.org/10.1007/BF00925710

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  • DOI: https://doi.org/10.1007/BF00925710

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