Allergen extract of horse hair and dandruff. Quantitative immunoelectrophoretic characterization of the antigens.
Freeze-dried extract of horse hair and dandruff was obtained by extraction, centrifugation, dialysis and freeze-drying. Quantitative immunoelectrophoresis using rabbit antibodies revealed the extract to be composed of 25 antigens of which some were mutually partial identical; 4 were serum-specific and non showed partial identity to solubilized hair proteins. Partial identity to antigens to serum and extract from hair and dandruff of cow, dog, cat, guinea pig, and of extract from house duct was demonstrated. After subjecting the extract to dialysis, ultrafiltration, freeze-drying and storage below 37degreesC for not more than 24 h the antigenic stability and the allergenic activity were unaffected. The effect of enzymatic degradation of the individual proteins with regard to antigenic stability and allergenic activity was also examined.
D000485:Allergens / Q000032:analysis*; D000818:Animals; D000941:Antigens / Q000032:analysis*; D002415:Cats; D002417:Cattle; D003956:Dialysis; D004285:Dogs; D004391:Dust; D005612:Freeze Drying; D006168:Guinea Pigs; D006197:Hair / Q000276:immunology*; D006736:Horses; D007122:Immunoelectrophoresis; D010447:Peptide Hydrolases / Q000494:pharmacology; D014020:Tissue Extracts / Q000276:immunology*; D014462:Ultrafiltration
D000485:Allergens; D000941:Antigens; D004391:Dust; D014020:Tissue Extracts; D010447:Peptide Hydrolases