Glycosylation-site-selective synthesis of N-acetyl-lactosamine repeats in bis-glycosylated human lysozyme

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • Ralph Melcher - , University of Marburg (Author)
  • Alexandra Hillebrand - , University of Marburg (Author)
  • Ute Bahr - , University Hospital Frankfurt (Author)
  • Bernd Schröder - , Institute of Physiological Chemistry, Inst. fur Physiologische Chemie, University of Marburg (Author)
  • Michael Karas - , University Hospital Frankfurt (Author)
  • Andrej Hasilik - , University of Marburg (Author)

Abstract

We have studied the elongation of oligosaccharides containing N-acetyl-lactosamine repeats using glycosylated human lysozyme mutants as a model. We reported previously that a combination of glycosylation sites at the 49th (site IV) and 68th (site II) amino acid residues of the protein particularly stimulates the synthesis of N-acetyl-lactosamine repeats. In the present study we show that it is the carbohydrate attached to site IV that is selectively affected. It contains more N-acetyl-lactosamine repeats when site II is glycosylated in the same molecule. As a corollary of the glycosylation at site II, the synthesis of a third antenna at site IV is increased. The triantennary oligosaccharides at site IV contain more N-acetyl-lactosamine repeats than the biantennary ones. Thus placing a carbohydrate at site II stimulates the branching and the elongation of the carbohydrate at the other site.

Details

Original languageEnglish
Pages (from-to)507-515
Number of pages9
JournalBiochemical journal
Volume348
Issue number3
Publication statusPublished - 15 Jun 2000
Peer-reviewedYes

External IDs

PubMed 10839980

Keywords

Keywords

  • Mutant, Oligosaccharide, Polylactosamine