Title of article
Purification and Characterization of Bovine Serum Albumin Using Chromatographic Method
Author/Authors
Balkani، Sanaz نويسنده Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran. , , Shamekhi، Sara نويسنده Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran , , Raoufinia، Ramin نويسنده Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran , , Parvan، Reza نويسنده Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran. , , Abdolalizadeh، Jalal نويسنده Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran. ,
Issue Information
دوفصلنامه با شماره پیاپی 0 سال 2016
Pages
4
From page
651
To page
654
Abstract
Purpose: Albumin is an abundant protein of blood and has many biopharmaceutical applications. The aim of this study was to purify bovine serum albumin (BSA) using produced rabbit anti-BSA antibody. Methods: The polyclonal antibody was produced against the BSA in rabbits. Then, the pure BSA was injected to three white New Zealand rabbits. ELISA test was done to evaluate antibody production. After antibody purification,the purified antibody was attached to CNBr-activated sepharose and finally it was used for purification of albumin from bovine serum. Western blotting analysis was used for functional assessment of immunoaffinity purified BSA. Results: The titer of anti-bovine albumin determined by ELISA was obtained 1: 256000. The SDS-PAGE showed up to 98% purity of isolated BSA and western blotting confirmed the BSA functionality. Purified bovine serum albumin by affinity chromatography showed a single band with molecular weight of 66 KDa. Conclusion: Affinity chromatography using produced rabbit anti-BSA antibody would be an economical and safe method for purification of BSA.
Journal title
Advanced Pharmaceutical Bulletin
Serial Year
2016
Journal title
Advanced Pharmaceutical Bulletin
Record number
2398977
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