A glycoprotein multimer from Bacillus thuringiensis sporangia: Dissociation into subunits and sugar composition
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 conditi...
Guardado en:
| Autores principales: | , |
|---|---|
| Formato: | JOUR |
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_03008177_v145_n1_p29_GarciaPatrone |
| Aporte de: |
| id |
todo:paper_03008177_v145_n1_p29_GarciaPatrone |
|---|---|
| record_format |
dspace |
| spelling |
todo:paper_03008177_v145_n1_p29_GarciaPatrone2023-10-03T15:17:41Z A glycoprotein multimer from Bacillus thuringiensis sporangia: Dissociation into subunits and sugar composition García-Patrone, M. Tandecarz, J.S. 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 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. Fil:Tandecarz, J.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03008177_v145_n1_p29_GarciaPatrone |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 García-Patrone, M. Tandecarz, J.S. A glycoprotein multimer from Bacillus thuringiensis sporangia: Dissociation into subunits and sugar composition |
| topic_facet |
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 |
| description |
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. |
| format |
JOUR |
| author |
García-Patrone, M. Tandecarz, J.S. |
| author_facet |
García-Patrone, M. Tandecarz, J.S. |
| author_sort |
García-Patrone, M. |
| title |
A glycoprotein multimer from Bacillus thuringiensis sporangia: Dissociation into subunits and sugar composition |
| title_short |
A glycoprotein multimer from Bacillus thuringiensis sporangia: Dissociation into subunits and sugar composition |
| title_full |
A glycoprotein multimer from Bacillus thuringiensis sporangia: Dissociation into subunits and sugar composition |
| title_fullStr |
A glycoprotein multimer from Bacillus thuringiensis sporangia: Dissociation into subunits and sugar composition |
| title_full_unstemmed |
A glycoprotein multimer from Bacillus thuringiensis sporangia: Dissociation into subunits and sugar composition |
| title_sort |
glycoprotein multimer from bacillus thuringiensis sporangia: dissociation into subunits and sugar composition |
| url |
http://hdl.handle.net/20.500.12110/paper_03008177_v145_n1_p29_GarciaPatrone |
| work_keys_str_mv |
AT garciapatronem aglycoproteinmultimerfrombacillusthuringiensissporangiadissociationintosubunitsandsugarcomposition AT tandecarzjs aglycoproteinmultimerfrombacillusthuringiensissporangiadissociationintosubunitsandsugarcomposition AT garciapatronem glycoproteinmultimerfrombacillusthuringiensissporangiadissociationintosubunitsandsugarcomposition AT tandecarzjs glycoproteinmultimerfrombacillusthuringiensissporangiadissociationintosubunitsandsugarcomposition |
| _version_ |
1807315136561545216 |