Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: Mass spectrometric analysis of electrophoretically separated allergens and proteases in grass pollen diffusates. | Respiratory Research BioMed Central Research Open Access Mass spectrometric analysis of electrophoretically separated allergens and proteases in grass pollen diffusates Mark J Raftery Rohit G Saldanha Carolyn L Geczy and Rakesh K Kumar Address Department of Pathology School of Medical Sciences University of New South Wales Sydney Australia 2052 Email Mark J Raftery - Rohit G Saldanha - Carolyn L Geczy - Rakesh K Kumar - Corresponding author Published 20 September 2003 Received 29 May 2003 Accepted 20 September 2003 Respiratory Research 2003 4 10 This article is available from http content 4 1 10 2003 Raftery et al licensee BioMed Central Ltd. This is an Open Access article verbatim copying and redistribution of this article are permitted in all media for any purpose provided this notice is preserved along with the article s original URL. Abstract Background Pollens are important triggers for allergic asthma and seasonal rhinitis and proteases released by major allergenic pollens can injure airway epithelial cells in vitro. Disruption of mucosal epithelial integrity by proteases released by inhaled pollens could promote allergic sensitisation. Methods Pollen diffusates from Kentucky blue grass Poa pratensis rye grass Lolium perenne and Bermuda grass Cynodon dactylon were assessed for peptidase activity using a fluorogenic substrate as well as by gelatin zymography. Following one- or two-dimensional gel electrophoresis Coomassie-stained individual bands spots were excised subjected to tryptic digestion and analysed by mass spectrometry either MALDI reflectron TOF or microcapillary liquid chromatography MS-MS. Database searches were used to identify allergens and other plant proteins in pollen diffusates. Results All pollen diffusates tested exhibited peptidase activity. Gelatin zymography revealed high Mr proteolytic activity at 95 000 in all .
