The allergens of dog II. Identification and partial purification of a major dander allergen

Authors

  • A. W. FORD,

    Corresponding author
    1. National Institute for Biological Standards and Control, Potters Bar and Department of Medicine, United Dental and Medical Schools of Guy's and St Thomas' Hospitals, St Thomas Street, London
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  • D. M. KEMENY

    1. National Institute for Biological Standards and Control, Potters Bar and Department of Medicine, United Dental and Medical Schools of Guy's and St Thomas' Hospitals, St Thomas Street, London
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Dr A. W. Ford, Standards Processing Division, National Institute for Biological Standards and Control, Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3QG.

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.

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