Structural analysis of the asparagine-linked oligosaccharides of human complement component C3
- 15 January 1986
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 233 (2) , 613-616
- https://doi.org/10.1042/bj2330613
Abstract
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 composition (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.This publication has 25 references indexed in Scilit:
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