Site-specific glycosylation analysis of human apolipoprotein B100 using LC/ESI MS/MS.

@article{Harazono2005SitespecificGA,
  title={Site-specific glycosylation analysis of human apolipoprotein B100 using LC/ESI MS/MS.},
  author={Akira Harazono and Nana Kawasaki and Toru Kawanishi and Tsunetoshi Hayakawa},
  journal={Glycobiology},
  year={2005},
  volume={15 5},
  pages={
          447-62
        }
}
Human apolipoprotein B100 (apoB100) has 19 potential N-glycosylation sites, and 16 asparagine residues were reported to be occupied by high-mannose type, hybrid type, and monoantennary and biantennary complex type oligosaccharides. In the present study, a site-specific glycosylation analysis of apoB100 was carried out using reversed-phase high-performance liquid chromatography coupled with electrospray ionization tandem mass spectrometry (LC/ESI MS/MS). ApoB100 was reduced, carboxymethylated… CONTINUE READING
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