Article - 
Limited access to UNIGEOther version: http://onlinelibrary.wiley.com/doi/10.1080/15216549700204461/pdf
Highlights
Home
Titles listCarbohydrate moiety of Plasmodium falciparum glycoproteins: the nature of the carbohydrate-peptide linkage...
Titles listCarbohydrate moiety of Plasmodium falciparum glycoproteins: the nature of the carbohydrate-peptide linkage...
Scientific Article
unige:11076 
 |
Carbohydrate moiety of Plasmodium falciparum glycoproteins: the nature of the carbohydrate-peptide linkage in the MSP-2 glycoprotein |
|
| Authors | ||
| Published in | Biochemistry and molecular biology international. 1997, vol. 43, no. 3, p. 655-668 | |
| Abstract | Metabolic labelling of Plasmodium falciparum parasites with [3H]GlcN, [3H]Man, [3H]Gal and [3H]ethanolamine, and subsequent purification by SDS-PAGE of the labelled material provided effective labelling of the MSP-1, 195 kDa, and MSP-2, 42-53 kDa, glycoproteins. Reductive beta-elimination of the MSP-2 released from the gel consisted of glycopeptides containing labelled sugars. Processing of the eliminated components and identification of the sugar residues demonstrated the presence of N-acetylglucosaminitol and N-acetylgalactosaminitol amongst other labelled sugars. Reductive beta-elimination with sodium hydroxide-sodium borotritide-borohydride showed the presence of glucosaminitol and alanine in the hydrolysis products. The MSP-2 was retained on solid phase wheat-germ agglutinin and was released from the lectin by treatment with GlcNAc. Upon treatment with O-glycanase the MSP-2 glycoprotein released labelled amino sugar, and derived oligosaccharides on treatment with exoglycosidases released labelled components corresponding to the metabolically incorporated sugars. Labelled Gal was incorporated into the MSP-2 glycoprotein using [3H]UDP-Gal and galactosyltransferase. The galactosylated glycoprotein released labelled Gal upon treatment with beta-galactosidase. The results of the present study suggest that the carbohydrate chains of the MSP-2 glycoprotein are attached to the protein backbone via GlcNAc- and GalNAc-serine/threonine in O-glycosyl linkage and the glycoprotein has terminal GlcNAc and Gal residues. The carbohydrate moieties of MSP-2, glycoprotein consist mainly of short chains linked to the protein core. | |
| Keywords | Animals — Antigens, Bacterial — Bacterial Outer Membrane Proteins — Bacterial Proteins/ chemistry/metabolism — Carbohydrates/ analysis — Chromatography/methods — Glycoproteins/ chemistry/metabolism — Glycosylation — Plasmodium falciparum/ chemistry/metabolism — Precipitin Tests — Protozoan Proteins/ chemistry/metabolism | |
| Identifiers | PMID: 9352084 | |
| Full text |
Article - Limited access to UNIGE Other version: http://onlinelibrary.wiley.com/doi/10.1080/15216549700204461/pdf |
|
| Citation (ISO format) | KHAN, A. H. et al. Carbohydrate moiety of Plasmodium falciparum glycoproteins: the nature of the carbohydrate-peptide linkage in the MSP-2 glycoprotein. In: Biochemistry and molecular biology international, 1997, vol. 43, n° 3, p. 655-668. https://archive-ouverte.unige.ch/unige:11076 |
415 hits 
0 download 
Contact an author
Update