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High-performance anion-exchange chromatography of asparagine-linked oligosaccharides

✍ Scribed by E. Watson; A. Bhide; W.C. Kenney; F.-K. Lin

Publisher: Elsevier Science
Year: 1992
Tongue: English
Weight: 609 KB
Volume: 205
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(92)90583-s

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✦ Synopsis

Oligosaccharides released enzymatically by N-glycanase from fetuin, alpha-acid glycoprotein, human chorionic gonadotropin, platelet-derived growth factor, and kallikrein were chromatographed on a polymeric pellicular anion-exchange column at pH values of 5 and 13. Separations occurred into groups of peaks containing the same number of sialic acids with an additional separation dependent upon the nature of the antennary structure present. High pH conditions were required for the optimum separation of fetuin oligosaccharides, while low pH conditions significantly improved resolution of oligosaccharides obtained from the other glycoproteins. The analytical separation of oligosaccharides under conditions of low pH has important implications in the development of chromatographic mapping and identification techniques for N-linked oligosaccharides present on recombinant proteins.

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