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   isolation and purification of hla-dr antigen from daudi cell line by immunoaffinity chromatography  
   
نویسنده khayyati zahra ,yari fatemeh
منبع journal of basic research in medical sciences - 2017 - دوره : 4 - شماره : 3 - صفحه:34 -38
چکیده    Introduction: the major histocompatibility complex (mhc) is a group of cell surface proteins that are essential for recognizing foreign molecules in human and other mammals. the physiologic function of mhc molecules is the presentation of peptides to t cells. in this study, we evaluated the purification of a class ii mhc molecule (hla-dr) from a human burkitt′s lymphoma cell line; daudi. materials and methods: we described a simple procedure for purifying human hla molecules from the cells lysate. as a representative model, hla-dr was purified from daudi cell line. the cell membrane was solubilized by a buffer contained np-40 detergent. subsequently, the isolation of the membrane antigen was carried out by affinity chromatography method using mouse anti-human hla-dr monoclonal antibody. the size and the specificity of the purified antigen were determined by bradford and elisa methods, respectively. results: the purified hla antigen was obtained in approximately 20-30 micrograms in each run of chromatography. additionally, elisa method demonstrated the hla-dr specificity of the purified protein. conclusion: the results indicated that affinity purification of hla-dr antigen by means of specific monoclonal antibody is a simple and fast procedure for obtaining the purified antigen.
کلیدواژه hla-dr ,affinity chromatography ,elisa
آدرس high institute for research and education in transfusion medicine, blood transfusion research center, ایران, high institute for research and education in transfusion medicine, blood transfusion research center, ایران
پست الکترونیکی f.yari@ibto.ir
 
     
   
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