BACKGROUND: Mugwort is the important source of fall allergic symptoms in the Mongolia. Mugwort pollen allergicpatients frequently present allergic symptoms of ingestion after several kinds of foods.OBJECTIVE: We sought to study the clinical manifestations of airag (fermented mare’s milk) and mare’s milkhypersensitivity in patients with mugwort allergy, identify the molecular weight of allergens, andevaluate their IgE cross-reactivity.MATERIAL AND METHODS: We collected to mugwort pollens from around UB in august and practiced fresh airag and mare’s milk.Airag, mare’s milk and mugwort extracts prepared by Hames Richmond method and their allergenswere identified by means of SDS-PAGE. ELISA inhibition experiments were done to study crossreactivitybetween airag and mugwort.RESULTS: In SDS-PAGE determined mugwort allergen 12-43 kDa, mare’s milk allergen 13-70 kDa, airag allergen12-68 kDamolecular weight.The study of the cross-reactivity between mugwort allergens and some food allergens was becamepractical significance on diagnosis, treatment and prevention of respiratory allergies. We were definedallergenic cross-reactivity between airag allergens and mugwort allergens which are common causesof upper respiratory allergy. On the Mugwort-ELISA inhibition test, the 50 % inhibitory dose to MugwortspecificIgE was 0.01μg/ml Mugwort allergens and 0.025μg/ml Airag allergens.However, the 1.0 μg/mlof Mugwort and Airag allergens were completely inhibited to Mugwort-specific IgE and Airag-specificIgE antibodies.CONCLUSION: In determined the mugwort pollen has 5 band(12, 23, 28, 38, 43kDa), in mare’s milk (13, 15, 60, 70кДа) and airag(12, 30, 50, 68 кДа) has separately 4 bands allergen protein by SDS-PAGE. ELISAinhibition study was strong cross-reactivity between airag allergen and mugwort allergen.

Introduction: Prevalence of asthma is increasing year by year, especially among children and exposure to high levels of indoor allergens is a very important factor [1]. Cockroaches are an important cause of asthma in many other regions of the world, including Taiwan, Thailand and Singapore in the Pacific Rim, Costa Rica and Puerto Rico in Centrel America, India, South Africa and more recently, Europe [2]. Goal: The aim of this study was determined total protein amounts allergenic proteins and protein bands of сockroach.Material and Methods: The сockroachs were collected in Ulaanbaatar. The allergenic protein components of the сockroach was purified by the method of Hames Richmond. The total protein of extracts was measured by the Bradford method and the protein components of cockroach were determined by the SDS-PAGE.Results: Among the 4000 known species of cockroaches, only 5 commonly inhabit homes and have the potential to contribute to indoor allergens. These include the American (periplaneta americana), German (Blattella germanica), Oriental (Blatta orientals), Smokey brown (Periplaneta fuliginosa), and brownbanded (Supella longipalpis) varieties [3]. We were defined 2,25mg/ml protein amounts (w/v) in extracts of the purified and lyophilized protein of the сockroach. We were used a standard marker 195,7; 104,0; 59,8; 41,6; 27,8; 21,1; 15,2; 6,5kd molecular weight proteins on the 13% separation gel of SDS-PAGE. On column determined protein bands with 82,3; 59,9; 55,2; 44,0; 41,6; 34,4, 22,7, 17,1 kd molecular weights.Conclusions: The сockroach was included 8 allergenic protein components between ranges of 17,1-82,3 kd molecular weights were determined in the extracts of the body Blatella germanica.

Background: The prevalence and incidence of allergic rhinitis is increasing in the last years in the Asia Pacific countries and for this reason, the number of research in aeroallergen and aeropollinology increasing. It depends on changes of geography, weather and plants, pollination period of time and air pollution.Goal: The aim of this study was determined allergenic characterization of proteins detected from Bromus inermis pollen.Mаterials and Methods: To define morphologic characteristics of Bromus inermis grass pollen and allergenic protein amounts’ of pollen and protein components.- The pollen morphologic characteristics of the Bromus inermis were defined and measured by optic microscopy (Aristoplan, Leitz, Germany).- The allergenic protein components of the Bromus inermis pollen were purified by the method of Hames, Richmond- Protein contents were measured by the Bradford method- The protein components of Bromus inermis pollen were determined by the SDS-PAGEResults and discussion:The diameter of the B.inermis dry pollen were mean length 41, 5±2, 3 μm and mean wide 32, 3±4, 1 μm. B.inermis dry pollen has oval and sphere shape and concaved on 3 sides with diameter 32.3-41.5 μm and was similar results one of subfamily of the Gramineae, Poaceae pollen size were defined 22-80 μm in diameter and with oval and sphere shapes. We were defined 1.5±0.02 mg protein amounts in the 5mg/ml extracts of the purified of the Bromus inermis pollen. Researcher [3] determined 1, 45 mg/ml protein on Elymus chinensis, 1, 96 mg/ml protein on Artimesia sieversiana, 3, 29 mg/ ml protein on Chenopodium album allergens. These study results are similar with our study result on Bradford method. We were defined 7 bands with 12, 26, 32, 55, 66, 84, 97 kDa molecular weight protein components. SDS-PAGE were deteсted relatively bright bands of 12, 32, 55, 66 kDa molecular weight protein components of Bromus inermis pollen proteins. Researcher Kaiser M et al were defined 16, 30, 40, 47, 50, 57, 60, 67, 70, 90, 95 and 110 kDa molecular weight bands in Lolium perenne pollen allergens. These study results are similar with our study result on SDS-PAGE. Conclusions:- The pollen of Bromus inermis was oval and sphere shapes with 32.3-41.5 μm in diameter.- We were defined 1.5±0.02 mg protein amounts in the 1mg/ml of the Bromus inermis pollen.- The 7 bands with 12, 26, 32, 55, 66, 84, 97 kDa molecular weight protein components of Bromus inermis pollen. SDS-PAGE were deteсted relatively bright bands of 12, 32, 55, 66 kDa molecular weight protein components.