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Glycoconjugate Journal

, Volume 15, Issue 10, pp 987–993 | Cite as

Increased elongation of N-acetyllactosamine repeats in doubly glycosylated lysozyme with a particular spacing of the glycosylation sites

  • Ralph Melcher
  • Hans-Wilhelm Grosch
  • Oliver Grosse
  • Andrej Hasilik
Article

Abstract

Lysozyme is an example of an extensively studied secretory enzyme. Glycosylated mutant human lysozyme has been used as a model in studies on the biosynthesis of N-acetyllactosamine repeats in N-linked oligosaccharides. We examined the biosynthesis of the repeats in two doubly glycosylated mutants and describe here a rapid purification and separation of singly and doubly glycosylated molecules. In one of the mutants, the elongation of the repeats is enhanced if the molecules are doubly glycosylated, but not if the carbohydrate is attached to either site individually. This enhancement is not seen in the other doubly glycosylated mutant. Since lysozyme is not structurally related to glycoproteins bearing carbohydrate with N-acetyllactosamine repeats, we propose that in multivalent substrates the synthesis of the repeats can be promoted by a proper spacing of the elongated carbohydrate antennae in addition to any role of the protein backbone.

Keywords

Carbohydrate Oligosaccharide Lysozyme Glycosylation Site Secretory Enzyme 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Kluwer Academic Publishers 1998

Authors and Affiliations

  • Ralph Melcher
    • 1
  • Hans-Wilhelm Grosch
    • 1
  • Oliver Grosse
    • 1
  • Andrej Hasilik
    • 1
  1. 1.Institute of Physiological ChemistryPhilipps-Universität MarburgMarburgGermany

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