Hydrophobic interaction chromatography for isolation and purification of Equ.cl, the horse major allergen

Abstract

Equ.cl, the horse ( Equus caballus) major allergen, was identified in a partially purified extract obtained from a crude aqueous horse dander extract, by acetonic precipitation and a salting-out process. It was isolated and purified by size-exclusion chromatography followed by hydrophobic interaction chromatography. Equ.cl appeared as an almost pure protein in a fraction eluted at 1.2 M ammonium sulphate from a phenyl Superose column. It is a single peptide with a relative molecular mass of 20 000 and a p I of ca. 3.9.