Interactions of concanavalin A with a trimannosyl oligosaccharide fragment of complex and high mannose type glycopeptides.
It has previously been reported that the binding interactions of concanavalin A with a purified high mannose type glycopeptide from ovalbumin differs from that with simple mono- and oligosaccharides (Brewer, C.F. (1979) Biochem. Biophys. Res. Commun. 90, 117-122). We now report studies with a synthetic analog of complex type glycopeptides, and a synthetic trimannosyl oligosaccharide fragment that is common to both complex and high mannose type glycopeptides. We find that both synthetic oligosacchardes undergo similar interactions with concanavalin A which mimic the effects of binding corresponding larger glycopeptides. Furthermore, the relative affinity of the trimannosyl oligosaccharide is 130-fold greater than the binding of methyl-alpha-D-mannopyranoside. The results indicate that the trimannosyl oligosaccharide is a unique structural element recognized by the lectin.
D003208:Concanavalin A / Q000378:metabolism*; D006020:Glycopeptides / Q000378:metabolism*; D006027:Glycosides / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008358:Mannose / Q000378:metabolism*; D008362:Mannosides / Q000378:metabolism*; D008766:Methylmannosides / Q000378:metabolism; D009844:Oligosaccharides / Q000378:metabolism
D006020:Glycopeptides; D006027:Glycosides; D008362:Mannosides; D008766:Methylmannosides; D009844:Oligosaccharides; D003208:Concanavalin A; C008466:methylmannoside; C044778:3,6-di-O-(alpha-mannopyranosyl)mannose; D008358:Mannose