Improved fractionation of sialylated glycopeptides by pellicular anion-exchange chromatography

Journal of Chromatography. a
J S Rohrer

Abstract

The glycoprotein bovine fetuin was treated with trypsin and the Asn-81 tryptic glycopeptide was purified (90% pure by Edman sequencing) by reversed-phase chromatography (RP-HPLC). The Asn-81 glycopeptide, which eluted as a single peak by RP-HPLC, was separable into five peaks on the NucleoPac PA100 column, a pellicular anion-exchange column. Each of the five Asn-81 glycopeptide peaks was shown to contain N-linked oligosaccharides by treatment of each peak with peptide N4-(N-acetyl-beta-D-glucosaminyl) asparagine amidase F (PNGase F) and subsequent oligosaccharide analysis by high-pH anion-exchange chromatography with pulsed amperometric detection. High-pH anion-exchange chromatography-pulsed amperometric detection oligosaccharide analysis revealed that each peak contained a different population of sialylated N-linked oligosaccharides. Hence each peak contained a different group of glycopeptide glycoforms. It was observed that the longer the retention time of the Asn-81 glycopeptide peak on the anion-exchange column, the greater the oligosaccharide sialylation. Two glycopeptide peaks which differed in their distribution of disialylated oligosaccharides demonstrated that the glycopeptide separation was a result of something more ...Continue Reading

References

Sep 8, 1992·Biochemistry·A TuongC Picard
Apr 25, 1992·Nucleic Acids Research·S M Gryaznov, R L Letsinger
Dec 1, 1991·Molecular Immunology·P M RuddR A Dwek
Jan 1, 1988·Annual Review of Biochemistry·T W RademacherR A Dwek
Mar 1, 1980·Proceedings of the National Academy of Sciences of the United States of America·J L Meek

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Citations

Sep 8, 2010·Biomedical Chromatography : BMC·Jennifer L Behan, Kevin D Smith

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