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The allergens of dog II. Identification and partial purification of a major dander allergen
Author(s) -
FORD A. W.,
KEMENY D. M.
Publication year - 1992
Publication title -
clinical and experimental allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 154
eISSN - 1365-2222
pISSN - 0954-7894
DOI - 10.1111/j.1365-2222.1992.tb02820.x
Subject(s) - allergen , isoelectric focusing , immunoglobulin e , chemistry , polyacrylamide gel electrophoresis , immunoelectrophoresis , staining , microbiology and biotechnology , isoelectric point , immunology , antibody , chromatography , biology , medicine , allergy , biochemistry , pathology , enzyme
Summary A dog hair and dander (DHD) extract was prepared from hair obtained from mixed breeds. By SDS‐polyacrylamide gel electrophoresis (SDS–PAGE) and immunoblotting, using sera from 32 dog‐allergic subjects, a number of IgE radio‐staining bands could be seen. In 78% of sera a protein of molecular weight (MW) of 21 000 daltons, designated Ag X, was found to bind IgE and in 34% it did so strongly. This allergen was isolated from DHD by size‐exclusion and ion exchange chromatography. The final product was a single allergen of MW of 21 000 and an isoelectric point of approximately 5.2. An additional protein‐staining band could still be seen of MW of 24 000 daltons. Using a serum which contained IgE antibodies only to Ag X, this allergen was found only in DHD extract and dog saliva and was absent from dog serum and urine. It was the same dog allergen that we [1] reported as Ag 8 using crossed radio‐immunoelectrophoresis (CRIE) and that Blands et al. [2] and Løwenstein [3] described as Ag 13. We propose that this major dog allergen be given the title Can f I according to the new allergen nomenclature.