Analysis of N- and O-glycosidically bound sialooligosaccharides in glycoproteins by high-performance liquid chromatography with pulsed amperometric detection.
N-Glycosidically bound sialooligosaccharides in a model glycoprotein of serum type (porcine thyroglobulin) were released by pronase digestion, followed by hydrazinolysis. The resulting oligosaccharides were re-N-acetylated and reduced with sodium borohydride. On the other hand, O-glycosidically bound sialooligosaccharides were released from a mucin-type glycoprotein (bovine submaxillary mucin) with alkali in the presence of sodium borohydride. The reduced oligosaccharides thus obtained from both types of glycoproteins were analysed by high-performance liquid chromatography on a column of a latex-type pellicular anion-exchange resin with strong alkali as eluent. These sequential procedures were useful for mapping of oligosaccharides in glycoproteins.
Honda
S
S
Faculty of Pharmaceutical Sciences, Kinki University, Higashi-osaka, Japan.
Suzuki
S
S
Zaiki
S
S
Kakehi
K
K
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D004553:Electric Conductivity; D006023:Glycoproteins / Q000032:analysis*; D009077:Mucins / Q000032:analysis; D009844:Oligosaccharides / Q000032:analysis*; D013552:Swine; D013954:Thyroglobulin / Q000032:analysis
D000596:Amino Acids; D006023:Glycoproteins; D009077:Mucins; D009844:Oligosaccharides; C016735:sialooligosaccharides; D013954:Thyroglobulin