Stability and mixing compatibility of dog epithelia and dog dander allergens

Abstract

Little information or data are available concerning the stability and compatibility of dog epithelia and dog dander allergens. To determine the immunochemical reactivities of commercial, nonstandardized dog epithelia and dog dander extracts after exposures to various temperatures or after mixing with high-protease fungal and cockroach extracts at concentrations recommended for maintenance immunotherapy (IT) injections. Quantitative enzyme-linked immunosorbent assay and qualitative (immunoblot) analyses were performed to compare specific compositional changes with total or individual allergen activities. Assays for dog allergens Can f 1 and Can f 3 (albumin) used specific mouse or rabbit antibodies. Multiallergen enzyme-linked immunosorbent assay inhibition and immunoblot methods were conducted using a human serum pool with high levels of IgE to dog allergens. Dog allergen recoveries ranged from 22% to 134% after short exposures to moderate or extreme temperatures and from 28% to 118% after mixing with fungal or insect extracts and storage for up to 15 months at 2 degrees C to 8 degrees C. Recoveries in dog dander extracts varied up to 2.5-fold with different test methods. Immunoblots revealed partial degradation of dog albumin molecules to discrete fragments that retained antibody-binding activities. In most cases, recoveries improved at elevated glycerin concentrations. Dog allergens in epithelia and dander extracts exhibited favorable temperature stabilities. Compatibilities with fungal or insect extracts may be compromised or at risk in some combinations. These data support current IT practice parameter recommendations of separating high-protease extracts from other products if possible; they also demonstrate that dog extracts possess allergen stabilities suitable for many IT formulations.