Comparative Studies on the Allergens of Horse Dandruff and Horse Serum

Abstract

Serum albumin was found to be an important allergen in horse epithelia extracts. The albumin concentration varied considerably, depending on the raw material used for the preparation of the allergen extracts. In addition to serum albumin, two allergenic proteins were demonstrated in horse dandruff. The molecular weights of these allergens were calculated to be about 38,000 and 22,000, respectively. The pi of the latter was 4.2. Fifty sera from allergic patients were studied by means of the radioallergosorbent test (RAST) using horse epithelia extract, horse dandruff extract, a purified horse dandruff allergen and horse serum as test allergens. About 24% of the patient sera studied were found to contain IgE specific to horse serum proteins. IgE specific to horse dandruff proteins was found in about 62% of the patient sera, while the rest, about 14%, apparently contained IgE specific to both kinds of allergens.

Comparative Study on Cat Allergens from Fur and Saliva

“…Immunoelectrophoretic and immunodiffusion analysis showed the presence of cat serum albumin. This serum protein could be responsible on the allerginicity of this frac tion and numerous reports indicate that albumin is an important allergen in horse [11] and dog [12] epithelia and to a lesser extent in cat extracts [2,4], The fraction with a mean molecular weight of 40.000 was resolved in two peaks of activity. One of them was associated with the protein band of pi 3.5.…”

Allergens of Horse Epithelium

“…Serum-related proteins in complex epithelial extracts were identified by using horse albumin and horse serum as markers in certain assays. In addition to previous studies [4,10,11 ] on horse epithelial extracts we extended our in vestigations to more recently developed methods, e.g. size exclusion high-performance liquid chromatogra phy (SE-HPLC) and immunoblotting methods.…”

“…To avoid ambiguous diagnostic results [6][7][8] or strong differences in allergenic activity between al lergen extracts from horse epithelia [9][10][11] not only the methods used for the extraction but also the source and the manufacturing process of the raw ma terial itself should be harmonized.…”

cDNA Cloning and Sequencing Reveal the Major Horse Allergen Equ c1 to Be a Glycoprotein Member of the Lipocalin Superfamily

“…The major horse allergen, Equ c1, is a potent allergen responsible for about 80% of anti-horse IgE antibody response in patients who are chronically exposed to horse allergens. Although much work has been carried out on the isolation and identification of the horse allergenic agents responsible for human hypersensitivity response (12)(13)(14)(15)(16), the major horse allergen was only recently purified from hair and dandruff (17). A previous study by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing-PAGE showed that Equ c1 appears as a single polypeptide with a relative molecular mass of 21,500 daltons and a pI of 3.9.…”