Grass pollens are one of the most important airborne allergen sources worldwide. The Poaceaefamily comprises about 9000 species, 20 species from five subfamilies are considered to be the mostfrequent causes of grass pollen allergy, and the allergenic relationships among them closely follow theirphylogenetic relationships. The allergic immune response to pollen of several grass species has beenstudied extensively over more than three decades. Eleven groups of allergens have been identified anddescribed, in most cases from more than one species. The most complete set of allergens has so farbeen isolated and cloned from Phleum pratense (timothy grass) pollen. Based on the prevalence of IgEantibody recognition among grass pollen-sensitized individuals, several allergens qualify as major, butmembers of two groups, groups 1 and 5, have been shown to dominate the immune response to grasspollen extract. Isoform variation has been detected in members of several of the allergen groups, whichin some cases can be linked to observed genetic differences. N-linked glycosylation occurs in membersof at least three groups. Carbohydrate- reactive IgE antibodies have been attributed to grass pollensensitization and found to cross-react with glycan structures from other allergen sources, particularlyvegetable foods. Another cause of extensive cross-reactivity are the group 12 allergens (profilins), whichbelong to a family of proteins highly conserved throughout the plant kingdom and present in all tissues.Members of eight allergen groups have been cloned and expressed as recombinant proteins capableof specific IgE binding. This development now allows diagnostic dissection of the immune response tograss pollen with potential benefits for specific immunotherapy.

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.