Volume 3, Issue 9 (2-2013)                   NCMBJ 2013, 3(9): 61-66 | Back to browse issues page

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Ghafari F, Kheirandish F, Kazemi B, Ghafari M D, Bandehpour M. Expression of recombinant human serum albumin in E.coli (BL21). NCMBJ 2013; 3 (9) :61-66
URL: http://ncmbjpiau.ir/article-1-288-en.html
Cellular and Molecular Biology Research Center, Shahid Beheshti University of Medical Sciences,Tehran,Iran and Biotechnology Departement, School of Medicine, Shahid Beheshti University of Medical Sciences,Tehran,Iran , bandehpour@gmail.com
Abstract:   (32020 Views)

Aims and Background. Human serum albumin (HSA) is the most important components of the circulatory system. HSA can transport many metabolites and hormones in the body . It is effective for blood volume stabilization and the burn treatment. The preparation of HSA from human plasma is costly and the risk of contamination with various pathogens is high. Therefore, biotechnology could promise a new way to solve the problems.

Materials and methods. HSA gene was synthesized based on the sequence of the gene in NCBI website . HSA was cloned into pET 22 b expression vector and then t he recombinant plasmid was transformed into BL21 (DE3) competent cell . The colony (containing recombinant expression vector) was cultured overnight. The culture was induced with IPTG 1/5 mM in the logarithmic phase (OD600=0.6). Sampling was carried out in different times and it was analyzed on %10 (w/v) SDS-PAGE. The expression of recombinant human serum albumin (rHSA) was confirmed by western blot. Finally, rHSA was Alpha purified by affinity chromatography.

Results.In this study, human serum albumin was produced in the bacterial periplasmic environment.  The highest expression level of rHSA was observed 24 h after the bacterial induction.

Conclusion.  In this study, rHSA was produced in E.coli host.

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Type of Study: Research Article | Subject: Biochemistry
Received: 2013/02/16 | Published: 2013/02/15

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