title: A glycoprotein multimer from Bacillus thuringiensis sporangia: dissociation into subunits and sugar composition.
abstract: 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.
authors.affiliation: Instituto de Investigaciones Bioquímicas, Fundación Campomar, Buenos Aires, Argentina.
authors.forename: M
authors.initials: M
authors.lastname: García-Patrone
authors.forename: J S
authors.initials: JS
authors.lastname: Tandecarz
mesh_terms: D001413:Bacillus thuringiensis / Q000737:chemistry*; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D002854:Chromatography, Paper; D004591:Electrophoresis, Polyacrylamide Gel; D005947:Glucose / Q000378:metabolism; D006023:Glycoproteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D009844:Oligosaccharides / Q000737:chemistry*; D011402:Pronase / Q000378:metabolism; D011487:Protein Conformation; D012694:Serine / Q000378:metabolism; D013171:Spores, Bacterial; D013997:Time Factors
chemical_list: D001426:Bacterial Proteins; D006023:Glycoproteins; D009844:Oligosaccharides; D012694:Serine; D011402:Pronase; D005947:Glucose