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

Carbohydr Res. 2000 Jan 12;323(1-4):111-25. doi: 10.1016/s0008-6215(99)00254-2.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amine Oxidase (Copper-Containing) / chemistry*
  • Animals
  • Carbohydrate Sequence
  • Chromatography, Ion Exchange
  • Electrophoresis, Capillary
  • Glycoside Hydrolases / chemistry
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Kidney / enzymology
  • Molecular Sequence Data
  • Oligosaccharides / chemistry*
  • Polysaccharides / chemistry
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Swine
  • Time Factors


  • Oligosaccharides
  • Polysaccharides
  • Amine Oxidase (Copper-Containing)
  • Glycoside Hydrolases