Structures of the asparagine-linked oligosaccharides of guinea-pig factor B of the alternative complement pathway.
This paper describes the structures of the asparagine-linked oligosaccharides of two forms of guinea-pig Factor B of the alternative complement pathway with different Mr values. Oligosaccharides were quantitatively liberated from both glycoproteins by hydrazinolysis, fractionated by paper electrophoresis and Bio-Gel P-4 column chromatography, and their structures determined by sequential exoglycosidase digestions in conjunction with methylation analysis. Both glycoproteins were shown to have the same biantennary complex-type oligosaccharides but it is suggested that they contain different numbers of oligosaccharide chains.
Mizuochi
T
T
Institute for Comprehensive Medical Science, Fujita Health University School of Medicine, Aichi, Japan.
Hamako
J
J
Titani
K
K
Matsushita
M
M
Okada
H
H
D000818:Animals; D001216:Asparagine; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D011415:Complement Factor B / Q000737:chemistry*; D003170:Complement Pathway, Alternative; D006168:Guinea Pigs; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry / Q000302:isolation & purification*
D009844:Oligosaccharides; D001216:Asparagine; D011415:Complement Factor B