On the variation of glycosylation in human plasma derived antithrombin.

@article{Demelbauer2005OnTV,
  title={On the variation of glycosylation in human plasma derived antithrombin.},
  author={Uwe M Demelbauer and Alexander Plematl and Djuro Josi{\'c} and G{\"u}nter Allmaier and Andreas M Rizzi},
  journal={Journal of chromatography. A},
  year={2005},
  volume={1080 1},
  pages={15-21}
}
The paper presents data on the primary structure of the glycan variants present in human antithrombin (AT) isoforms obtained from a plasma pool. The analysis is conducted on the level of glycopeptides gained by tryptic digestion. The glycopeptides were pre-separated by lectin-affinity chromatography and analyzed by means of electrospray ionization-tandem mass spectrometry involving collision-induced dissociation. Variations of the canonical biantennary complex-type structure were present with… CONTINUE READING