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isolation and purification of hla-dr antigen from daudi cell line by immunoaffinity chromatography
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نویسنده
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khayyati zahra ,yari fatemeh
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منبع
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journal of basic research in medical sciences - 2017 - دوره : 4 - شماره : 3 - صفحه:34 -38
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چکیده
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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.
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کلیدواژه
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hla-dr ,affinity chromatography ,elisa
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آدرس
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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
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پست الکترونیکی
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f.yari@ibto.ir
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Authors
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