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N-Linked oligosaccharide structures in the diamine oxidase from porcine kidney

Authors
Journal
Carbohydrate Research
0008-6215
Publisher
Elsevier
Publication Date
Volume
323
Identifiers
DOI: 10.1016/s0008-6215(99)00254-2
Keywords
  • Exoglycosidases
  • N-Glycan
  • Hpaec
  • Maldi/Tof-Ms
  • Porcine Kidney Diamine Oxidase
Disciplines
  • Biology

Abstract

Abstract 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.

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