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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. © 1995 Kluwer Academic Publishers.

Registro:

Documento: Artículo
Título:A glycoprotein multimer from Bacillus thuringiensis sporangia: Dissociation into subunits and sugar composition
Autor:García-Patrone, M.; Tandecarz, J.S.
Filiación:Instituto de Investigaciones Bioquímicas 'Fundación Campomar', Av. Patricias Argentinas 435, Buenos Aires, 1405, Argentina
Instituto de Inverstigaciones Bioquímicas, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina
Instituto de Investigaciones Bioquímicas Buenos Aires, CONICET, Argentina
Palabras clave:Bacillus thuringiensis; dissociation; glycoprotein; oligosaccharides; sporangium; glycoprotein; oligosaccharide; polymer; protein subunit; article; bacillus thuringiensis; carbohydrate metabolism; crystal structure; deglycosylation; dissociation; hydrophobicity; nonhuman; polyacrylamide gel electrophoresis; protein analysis; sugar transport; Bacillus thuringiensis; Bacterial Proteins; Chromatography, Gel; Chromatography, Ion Exchange; Chromatography, Paper; Electrophoresis, Polyacrylamide Gel; Glucose; Glycoproteins; Hydrogen-Ion Concentration; Oligosaccharides; Pronase; Protein Conformation; Serine; Spores, Bacterial; Support, Non-U.S. Gov't; Time Factors
Año:1995
Volumen:145
Número:1
Página de inicio:29
Página de fin:37
DOI: http://dx.doi.org/10.1007/BF00925710
Título revista:Molecular and Cellular Biochemistry
Título revista abreviado:Mol Cell Biochem
ISSN:03008177
CODEN:MCBIB
CAS:Bacterial Proteins; Glucose, 50-99-7; Glycoproteins; Oligosaccharides; Pronase, EC 3.4.24.-; Serine, 56-45-1
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v145_n1_p29_GarciaPatrone

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Citas:

---------- APA ----------
García-Patrone, M. & Tandecarz, J.S. (1995) . A glycoprotein multimer from Bacillus thuringiensis sporangia: Dissociation into subunits and sugar composition. Molecular and Cellular Biochemistry, 145(1), 29-37.
http://dx.doi.org/10.1007/BF00925710
---------- CHICAGO ----------
García-Patrone, M., Tandecarz, J.S. "A glycoprotein multimer from Bacillus thuringiensis sporangia: Dissociation into subunits and sugar composition" . Molecular and Cellular Biochemistry 145, no. 1 (1995) : 29-37.
http://dx.doi.org/10.1007/BF00925710
---------- MLA ----------
García-Patrone, M., Tandecarz, J.S. "A glycoprotein multimer from Bacillus thuringiensis sporangia: Dissociation into subunits and sugar composition" . Molecular and Cellular Biochemistry, vol. 145, no. 1, 1995, pp. 29-37.
http://dx.doi.org/10.1007/BF00925710
---------- VANCOUVER ----------
García-Patrone, M., Tandecarz, J.S. A glycoprotein multimer from Bacillus thuringiensis sporangia: Dissociation into subunits and sugar composition. Mol Cell Biochem. 1995;145(1):29-37.
http://dx.doi.org/10.1007/BF00925710