Abstract
The Asn-linked oligosaccharides of four different glycoproteins were cleaved by N-glycanase and analysed by high-pH anion-exchange high-performance liquid chromatography coupled with a pulsed amperometric detector. Each glycoprotein produced unique sets of oligosaccharides. Sialic acid-containing oligosaccharide peaks were readily identified by their large decrease in retention time following neuraminidase digestion. The use of this HPLC technique for tentatively identifying unknown oligosaccharide peaks by retention time comparison with reference standards and for monitoring the consistency of N-glycosylation of recombinant DNA-derived glycoprotein was demonstrated.
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