Carbohydrate structures of the glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen

J Biochem. 1995 Feb;117(2):289-95. doi: 10.1093/jb/117.2.289.

Abstract

The glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen was treated with pepsin and glycopeptidase A to release asparagine-linked oligosaccharides. The reducing ends of the oligosaccharides were aminated with the fluorescent reagent 2-aminopyridine. The oligosaccharide derivatives were purified by gel permeation chromatography and reversed-phase HPLC. Their structures were determined by sequential exoglycosidase digestion and 500 MHz 1H-NMR spectroscopy. Four oligosaccharide structures, A, B, C, and D, were identified as the xylose-containing complex-type. They were present at a molar ratio of 8:1:6:1. By amino acid sequence analyses of the tryptic peptides, Asn-170 and Asn-333 of Cry j I were found to carry asparagine-linked oligosaccharides. [formula: see text]

MeSH terms

  • Allergens / chemistry*
  • Amino Acid Sequence
  • Antigens, Plant
  • Asparagine
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Chromatography, High Pressure Liquid
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Oligosaccharides / chemistry*
  • Oligosaccharides / isolation & purification
  • Peptide Fragments / chemistry
  • Peptide Fragments / isolation & purification
  • Plant Proteins / chemistry*
  • Pollen / chemistry*
  • Trees
  • Trypsin
  • Xylose / analysis

Substances

  • Allergens
  • Antigens, Plant
  • Cry j I protein, Cryptomeria japonica
  • Oligosaccharides
  • Peptide Fragments
  • Plant Proteins
  • Asparagine
  • Xylose
  • Trypsin