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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-04

AUTHORS

M. García-Patrone, Juana S. Tandecarz

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. More... »

PAGES

29-37

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00925710

DOI

http://dx.doi.org/10.1007/bf00925710

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1004277946

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7659076


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