Serum Albumin – An Important Allergen in Dog Epithelia Extracts

The allergenic components of cat fur extract were localized in the molecular weight range 65,000–40,000 and had a pI of 3.9–5, except one with a more acid pI of 3.5. The fraction with a mean molecular weight of 65,000 contained proteins of pI 4.5–5 and mainly cat serum albumin. The fraction with a mean molecular weight of 40,000 showed two peaks of activity. One of them was associated with a protein of pI 3.5, and immunodiffusion analysis showed the presence of ‘Cat Allergen One’. A comparative study on cat saliva showed that the allergenic activity was restricted to proteins of the same molecular weight range. ‘Cat Allergen One’ was present in the fraction of molecular weight 40,000.

Section: Discussionmentioning

confidence: 91%

Comparative Study on Cat Allergens from Fur and Saliva

Didierlaurent

Foglietti

Guérin

et al. 1984

“…Dog dander antigen is quite heteroge neous and may contain several important antigenic components [6,7]. This factor along with the reported variability of poten cy and composition of commercially availa ble dog dander extracts would appear to make clinical use of this antigen extract somewhat difficult.…”

Section: Discussionmentioning

confidence: 99%

Clinical Comparison of Skin Testing and the Radioallergosorbent Test in Dog-Sensitive Patients Using Mixed and Breed-Specific Antigens

Meriney¹,

Wallace²,

Miller³

et al. 1979

A study of clinical history, intradermal test end points and RAST values with six different dog antigens was made in 20 patients and 5 control subjects. Skin testing was found to be more useful clinically than the RAST. Considerable variability among mixed epidermal extracts was noted. There was no apparent advantage to testing with three individual-breed extracts studied, compared to the most potent mixed epidermal antigen. The results of this study suggest that further efforts toward standardization of potency, methods of preparation and, possibly, breed composition of dog allergenic extracts are required to develop improved allergens for clinical use.

“…Loewenstein's general studies of mammalian allergens [1] revealed several dog allergens, Uhlin et al [2] demon strated 24 antigens, whereas Ford et al [3] lergens in dog hair/dander extracts. Some of these aller gens have been identified as serum components, like albu min (Ag3) and y-globulin (Ag23) (2], By means of gel filtration, two components around 28 kD were character ised by Yman et al [4] in dog dander extracts. Recently, a major allergen (Agl3) was purified by Schou et al [5] re vealing a molecular weight (MW) of 25 kD on SDS-PAGE and 22 kD by HPLC gel filtration.…”

Section: Introductionmentioning

confidence: 99%

Characterisation of Dog Allergens by Means of Immunoblotting

Spitzauer

Schweiger²,

Anrather³

et al. 1993

Sera from 75 patients with clinical type I allergy against dogs were investigated by means of immunoblotting using extracts prepared from dog hair/dander (CAN XI D) and saliva. In addition, selected sera were tested on extracts made of hair, skin, salivary glands (parotis and submandibularis), serum and liver. A 69-kD IgE-binding protein was identified in all extracts tested with an incidence of approximately 40% and shown to be dog albumin by means of inhibition experiments. In 96% of patients’ sera IgE antibodies reactive with a 19-kD and/or a 23-kD protein of the hair/dander extract (CAN XID) were observed. IgE binding to a 23-kD band was also detected in the hair and saliva extracts, but not in skin, salivary gland, serum and liver extracts. A 19-kD IgE-binding protein was strongly expressed in skin and to a lesser degree in saliva, but not in hair, serum and liver. Preincubation of patients sera with the hair extract and subsequent probing with the hair/dander extract (CAN XI D) inhibited IgE binding to the 23 kD protein whereas preincubation with the skin extract abolished IgE binding to the 19-kD protein. Using the hair/dander extract as inhibitor, IgE binding to the 19- and 23-kD proteins of saliva was abrogated. Thus it is concluded that the 23-kD protein is preferentially expressed in hair and saliva whereas the 19-kD protein is found in saliva and skin. Furthermore these two proteins are likely to represent immunologically independent major allergens.