Carbohydrate structure of human pancreatic elastase 1.
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.
Wendorf
P
P
Institut für Medizinische Mikrobiologie, Universität Giessen, Federal Republic of Germany.
Linder
D
D
Sziegoleit
A
A
Geyer
R
R
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006020:Glycopeptides / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008745:Methylation; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry* / Q000378:metabolism; D010179:Pancreas / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000737:chemistry* / Q000302:isolation & purification; D013402:Sugar Alcohols / Q000737:chemistry; D014357:Trypsin / Q000737:chemistry
D006020:Glycopeptides; D009844:Oligosaccharides; D013402:Sugar Alcohols; D010196:Pancreatic Elastase; D014357:Trypsin