Purification and characterization of the major dog allergen, Can f I
Article first published online: 27 APR 2006
Clinical & Experimental Allergy
Volume 21, Issue 3, pages 321–328, May 1991
How to Cite
SCHOU, C., SVENDSEN, U. G. and LøWENSTEIN, H. (1991), Purification and characterization of the major dog allergen, Can f I. Clinical & Experimental Allergy, 21: 321–328. doi: 10.1111/j.1365-2222.1991.tb01663.x
- Issue published online: 27 APR 2006
- Article first published online: 27 APR 2006
- Submitted 26 July 1990; resived 30 October 1990; accepted 22 November 1990.
An important dog-hair and dander-specific allergen Ag13 has been purified by means of immunoaffinity chromatography utilizing rabbit antibody specific for Ag13. Purity was judged to be very high as detected by crossed immunoelectrophoresis and SDS-PAGE. The purified allergen was subjected to amino acid analyses. Molecular weight was about 22 kD in HPLC-gel filtration and 25 kD in SDS PAGE with an additional band at 18 kD. In vitro IgE binding of the allergen was investigated by luminescence immunoassay (LIA) inhibition. Removal of Ag13 from dog hair and dander extract (DHD) removed 50 ± 1.5% of the IgE binding capacity. The purified allergen inhibited up to 56.5% of the IgE activity to DHD as measured with a pool of serum from dog-allergic patients. Out of 26 dog-allergic patients, 24 had a positive skin-prick test to the allergen. Out of 23 dog-allergic patients, 16 reacted with the allergen in IgE immunoblotting. We suggest that Ag13 be termed Can f I. The allergen will be a marker allergen for environmental dog hair and dander exposure.