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Structures of the asparagine-linked oligosaccharides of guinea-pig factor B of the alternative complement pathway

  • T. Mizuochi
  • , J. Hamako
  • , K. Titani
  • , M. Matsushita
  • , H. Okada

Research output: Contribution to journal › Article › peer-review

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 M(r) 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.

Original languageEnglish
Pages (from-to)533-535
Number of pages3
JournalBiochemical Journal
Volume272
Issue number2
DOIs
Publication statusPublished - 1990

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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