Characterization of isoforms of the major allergen Phl p V by two-dimensional immunoblotting and microsequencing

Int Arch Allergy Immunol. 1992;98(2):105-9. doi: 10.1159/000236172.

Abstract

Timothy pollen extract was separated by 2D PAGE blot for further characterization of the major allergen Phl p V. Using pooled patient serum, we demonstrated that Phl p V consists of 4 components at 32 kD and 4 components at 38 kD, each differing in their pIs. The primary structure and the amino acid composition of the 8 proteins were determined form the blotted samples. Proteins of the same molecular weight did not differ in the 20 N-terminal amino acid residues, whereas the 32- and 38-kD proteins showed only 60% sequence identity. Furthermore, the results of the amino acid analyses suggest differences in their protein structure. Therefore, it might be possible that both proteins express different IgE-reactive epitopes.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / chemistry*
  • Allergens / immunology
  • Amino Acid Sequence
  • Electrophoresis, Gel, Two-Dimensional
  • Humans
  • Immunoblotting
  • Molecular Sequence Data
  • Molecular Weight
  • Plant Proteins / chemistry
  • Plant Proteins / immunology*
  • Poaceae / immunology*
  • Pollen / chemistry
  • Pollen / immunology*

Substances

  • Allergens
  • Phl p V protein, Phleum pratense
  • Plant Proteins