Heterogeneity in utilization of N-glycosylation sites Asn624 and Asn138 in human lactoferrin: a study with glycosylation-site mutants.

Antzeko izenburuak

• Glycosylated and unglycosylated human lactoferrins both bind iron and show identical affinities towards human lysozyme and bacterial lipopolysaccharide, but differ in their susceptibilities towards tryptic proteolysis.
  nork: van Berkel, P H, et al.
  Argitaratua: (1995)
• N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA.
  nork: van Berkel, P H, et al.
  Argitaratua: (1997)
• Determination of Glycosylation Sites and Site-specific Heterogeneity in Glycoproteins
  nork: An, Hyun Joo, et al.
  Argitaratua: (2009)
• N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant Protein C
  nork: Gil, Geun-Cheol, et al.
  Argitaratua: (2009)
• Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: Function of the Asn–His interaction in the catalytic triad
  nork: Snijder, H.J., et al.
  Argitaratua: (2001)