TY - JOUR
T1 - Structure of the major oligosaccharide of cobra venom factor
AU - Gowda, D. Channe
AU - Schultz, Michael
AU - Bredehorst, Reinhard
AU - Vogel, Carl Wilhelm
N1 - Funding Information:
TM. Schultz was supported by a postdoctoral fellowship from the Deutsche Forschungsgemeinschaft (Schu 614/1-l). Current address: Boehringer Mannheim GmbH, 6800 Mannheim, Germany. $Current address: Department of Biochemistry and Molecular Biology, University of Hamburg, Hamburg, Germany. $Address for correspondence: Dr Carl-Wilhelm Vogel, Depart-ment of Biochemistry and Molecular Biology, University of Hamburg, Martin Luther King Pl. 6, 2000 Hamburg 13, Germany.
Funding Information:
*Preliminary accounts of this work were presented at the 72nd Annual Meeting of the Federation of American Societies for Experimental Biology, Las Vegas, Nevada, May 1988 and at the 19th Annual Meeting of the Society for Complex Carbohydrates, San Diego, California, October 1990. This work was supported by National Institutes of Health Grants HL 29523. AI 26821, and CA 01039.
PY - 1992/3
Y1 - 1992/3
N2 - Cobra venom factor (CVF), the complement-activating glycoprotein in cobra venom, contains three or possibly four N-linked oligosaccharide chains per molecule and is devoid of O-linked saccharides. Analysis by lectin-affinity staining revealed the presence of complex-type oligosaccharides containing non-reducing terminal α-galactosyl residues and fucose residues linked to the proximal N-acetylglucosamine. Sialic acid residues could not be detected. For their structural analysis, the oligosaccharides were released by hydrazinolysis and fractionated on Bio-Gel P-4. Approximately 80% of the eluted oligosaccharides have a size equivalent of 17 ± 2 glucose units. The major oligosaccharide representing about 45% of the total carbohydrate present in CVF was purified to homogeneity by MicroPak AX-5 HPLC and its structure was analyzed by sequential exoglycosidase digestion. The positions of the glycosidic linkages of the sugar residues were established by methylation analysis of CVF-derived glycopeptides. The data of these analyses indicated that the major oligosaccharide has a symmetrical fucosylated biantennary complex-type structure terminating with unusual α-galactosyl residues.
AB - Cobra venom factor (CVF), the complement-activating glycoprotein in cobra venom, contains three or possibly four N-linked oligosaccharide chains per molecule and is devoid of O-linked saccharides. Analysis by lectin-affinity staining revealed the presence of complex-type oligosaccharides containing non-reducing terminal α-galactosyl residues and fucose residues linked to the proximal N-acetylglucosamine. Sialic acid residues could not be detected. For their structural analysis, the oligosaccharides were released by hydrazinolysis and fractionated on Bio-Gel P-4. Approximately 80% of the eluted oligosaccharides have a size equivalent of 17 ± 2 glucose units. The major oligosaccharide representing about 45% of the total carbohydrate present in CVF was purified to homogeneity by MicroPak AX-5 HPLC and its structure was analyzed by sequential exoglycosidase digestion. The positions of the glycosidic linkages of the sugar residues were established by methylation analysis of CVF-derived glycopeptides. The data of these analyses indicated that the major oligosaccharide has a symmetrical fucosylated biantennary complex-type structure terminating with unusual α-galactosyl residues.
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U2 - 10.1016/0161-5890(92)90020-X
DO - 10.1016/0161-5890(92)90020-X
M3 - Article
C2 - 1557044
AN - SCOPUS:0026533188
SN - 0161-5890
VL - 29
SP - 335
EP - 342
JO - Molecular Immunology
JF - Molecular Immunology
IS - 3
ER -