The study of allergen’s protein of bromus inermis pollen / Монголын Анагаах Ухаан

ABSTRACT

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.