Biochemical characterization and surfactant properties of horse allergens

A new allergen from horse dander, Equ c 5 has been purified. Its biochemica l and biophysical properties have been characterized and compared with thos e of Equ c 1, Equ c 2 and Equ c 4. Their molecular masses, determined by ma ss spectrometry, were 22 kDa for Equ c 1, 16 kDa for Equ c 2, 18.7 kDa for Equ c 4 and 16.7 kDa for Equ c 5. Their pI values were between 3.8 and 5.25 . Equ c 2 and Equ c 5 are not glycosylated, while Equ c 4 contains a tri-an tennary tri-sialylated N-linked glycan. Linkages of terminal N-acetylneuram inic acid to galactose were: alpha-(2 -->6) in Equ c 4, and both alpha-(2 - ->3) and alpha-(2 -->6) in Equ c 1. Oligosaccharide portions of Equ c 1 or Equ c 4 were barely involved in IgE-immunoreactivity. Partial N-terminal se quence of Equ c 4 shares a significant sequence homology with the rat subma ndibular gland protein A. No matching was found for two internal peptides o f Equ c 5. Surfactant properties of horse allergens as well as other protei ns were investigated. In contrast to Equ c 2 and Equ c 3, solutions of Equ c 1, Equ c 4 and Equ c 5 significantly lowered the surface tension. Relatio nship between a property such as this, involving oriented hydrophobic patch es of a molecule and allergenicity, is addressed.