The multiplicity of N-glycan structures of bovine milk 18 kda lactophorin (milk GlyCAM-1)

Biosci Biotechnol Biochem. 2010;74(2):447-50. doi: 10.1271/bbb.90887. Epub 2010 Feb 7.


Lactophorin is a heat-stable phosphoglycoprotein, also known as milk glycosylation-dependent cell adhesion molecule 1 (GlyCAM-1). Bovine 18 kDa lactophorin was purified by heparin affinity chromatography from cow's milk whey. Its N-glycans were obtained by proteomic techniques, including two-dimensional polyacrylamide gel electrophoresis (2D-PAGE), followed by in-gel digestion with peptide-N(4)-(N-acetyl-beta-glucosaminyl)-asparagine amidase (PNGase F). The released N-glycans were derivatized with 2-aminopryridine (PA) and analyzed by matrix-assisted laser desorption ionization quadruple ion trap time of flight mass spectrometry (MALDI-QIT-TOF MS). Among the MS analyzed peaks, 15 peaks were found to be N-glycan molecules as detected by MS(2) analysis. These glycans consisted of mono-sialylated bi-, tri-, and tetra-antennary complex-type N-glycans carrying Gal-GlcNAc (LacNAc) or GalNAc-GlcNAc (LacdiNAc) with and without core-fucose.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Female
  • Milk Proteins / chemistry*
  • Molecular Weight
  • Mucins / chemistry*
  • Polysaccharides / chemistry*


  • Milk Proteins
  • Mucins
  • Polysaccharides
  • lactophorin protein, Bos taurus
  • sulfated glycoprotein p50