HYDROPHOBIC INTERACTION CHROMATOGRAPHY FOR ISOLATION AND PURIFICATIONOF EQU.CL, THE HORSE MAJOR ALLERGEN

Equ.c1, 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 wits isolated and purified by size-exclusion chromatography followed by hy drophobic interaction chromatography. Equ.c1 appeared as an almost pur e protein in a fraction eluted at 1.2 M ammonium sulphate from a pheny l Superose column. It is a single peptide with a relative molecular ma ss of 20 000 and a pI of ca. 3.9.