title: 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 pI of ca. 3.9.
authors.affiliation: Unité d'Immuno-Allergie, Institut Pasteur, Paris, France.
authors.forename: J P
authors.initials: JP
authors.lastname: Dandeu
authors.forename: J
authors.initials: J
authors.lastname: Rabillon
authors.forename: A
authors.initials: A
authors.lastname: Divanovic
authors.forename: A
authors.initials: A
authors.lastname: Carmi-Leroy
authors.forename: B
authors.initials: B
authors.lastname: David
mesh_terms: D000485:Allergens / Q000302:isolation & purification*; D000818:Animals; D002850:Chromatography, Gel; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006736:Horses / Q000276:immunology*; D007120:Immunochemistry; D007525:Isoelectric Focusing
chemical_list: D000485:Allergens