Physicochemical characterization of a major protein allergen, Der p I, from the house dust mite, Dermatophagoides pteronyssinus. Amino acid analysis and circular dichroism studies

Int Arch Allergy Appl Immunol. 1987;82(3-4):444-6. doi: 10.1159/000234249.

Abstract

A major house dust mite allergen, Der p I, was isolated from spent growth medium and physicochemically characterized. These studies show that the allergen is monomeric, contains approximately 216 residues and 4 intra-chain disulphide bonds. The N-terminal amino acid is threonine. Circular dichroism studies show that the allergen contains 10% alpha-helical, 50% beta-pleated sheet and 40% random structures.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / isolation & purification*
  • Amino Acids
  • Animals
  • Antigens, Dermatophagoides
  • Circular Dichroism
  • Mites / analysis*
  • Protein Conformation

Substances

  • Allergens
  • Amino Acids
  • Antigens, Dermatophagoides