Carbohydrate structure of human pancreatic elastase 1

Biochem J. 1991 Sep 1;278 ( Pt 2)(Pt 2):505-14. doi: 10.1042/bj2780505.


Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett. 249, 275-278]. In order to study its glycosylation, glycoprotein isolated from post-mortem pancreas tissue of 75 donors was digested with trypsin. Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration. Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases. The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Chromatography, Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Glycopeptides / metabolism
  • Glycosylation
  • Humans
  • Hydrogen-Ion Concentration
  • Methylation
  • Molecular Sequence Data
  • Oligosaccharides / chemistry*
  • Oligosaccharides / metabolism
  • Pancreas / enzymology*
  • Pancreatic Elastase / chemistry*
  • Pancreatic Elastase / isolation & purification
  • Sugar Alcohols / chemistry
  • Trypsin / chemistry


  • Glycopeptides
  • Oligosaccharides
  • Sugar Alcohols
  • Pancreatic Elastase
  • Trypsin