Structural analysis of the asparagine-linked oligosaccharides of human complement component C3

Biochem J. 1986 Jan 15;233(2):613-6. doi: 10.1042/bj2330613.


The asparagine-linked oligosaccharides of human C3 were characterized. The C3 oligosaccharides were released by endo-beta-N-acetylglucosaminidase H and were analysed by lectin affinity chromatography and h.p.l.c. The released oligosaccharides bound tightly to concanavalin A-Sepharose and were not retained by agarose-bound wheat-germ agglutinin, indicating that they were only of high-mannose type. Two major oligosaccharide structures were separated from both the alpha- and beta-chains of C3 by h.p.l.c. on Micropak AX-5, calibrated with high-mannose-type oligosaccharides of known structures. The oligosaccharide structures on the alpha-chain have the compositions (Man)9(GlcNAc)2-Asn and (Man)8 (GlcNAc)2-Asn, and those on the beta-chain have the compositions (Man)6(GlcNAc)2-Asn and (Man)5(GlcNAc)2-Asn.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Asparagine / analysis*
  • Chromatography, Affinity
  • Chromatography, High Pressure Liquid
  • Complement C3*
  • Humans
  • Mannosidases
  • Oligosaccharides / analysis*
  • alpha-Mannosidase


  • Complement C3
  • Oligosaccharides
  • Asparagine
  • Mannosidases
  • alpha-Mannosidase