N-linked oligosaccharide structures in the diamine oxidase from porcine kidney.
Structures of the N-linked glycans released from porcine kidney diamine oxidase (DAO) were characterized utilizing various analytical techniques, including matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI/TOF-MS), high-performance capillary electrophoresis (HPCE), and high-pH anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD). The oligosaccharide sequences present in DAO were conclusively determined using specific exoglycosidases in conjunction with MALDI/TOF-MS. The structures found in the glycoprotein are primarily linear, di-, or tribranched fucosylated complex type. MS analysis of the esterified N-glycan pool derived from DAO indicated the presence of several di- and trisialylated structures.
Huang
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Y
Department of Chemistry, Indiana University, Bloomington 47405, USA.
Mechref
Y
Y
Novotny
M V
MV
D006631:Amine Oxidase (Copper-Containing) / Q000737:chemistry*; D000818:Animals; D002240:Carbohydrate Sequence; D002852:Chromatography, Ion Exchange; D019075:Electrophoresis, Capillary; D006026:Glycoside Hydrolases / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007668:Kidney / Q000201:enzymology; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry*; D011134:Polysaccharides / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013552:Swine; D013997:Time Factors
D009844:Oligosaccharides; D011134:Polysaccharides; D006631:Amine Oxidase (Copper-Containing); D006026:Glycoside Hydrolases