Structures of the asparagine-linked oligosaccharides of guinea-pig factor B of the alternative complement pathway. |
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Authors: | T Mizuochi J Hamako K Titani M Matsushita H Okada |
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Affiliation: | Institute for Comprehensive Medical Science, Fujita Health University School of Medicine, Aichi, Japan. |
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Abstract: | 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. |
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