Volume 9, Issue 1 (2018)
JMBS 2018, 9(1): 79-92 |
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Ghasemi R, Hashemzadeh H, Razavi H, Yakhchali B. Production of Recombinant Human Growth Hormone and Future Challenges. JMBS 2018; 9 (1) :79-92
URL: http://biot.modares.ac.ir/article-22-14265-en.html
URL: http://biot.modares.ac.ir/article-22-14265-en.html
1- Department Nanobiotechnology, Bioscience Faculty, Tarbiat Modares University, Tehran, Iran
2- Nanobiotechnology Recearch Centre, Baqiyatallah University of Medical Sciences, Tehran, Iran
3- Department of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran, National Institute of Genetics & Biotechnology, Pajouhesh Boulevard, Town of Science & Technology Research, 15 Kilometer, Highway Tehran- Karaj, Tehran, Iran. Postal Code: 1497716316 ,bahar@nigeb.ac.ir
2- Nanobiotechnology Recearch Centre, Baqiyatallah University of Medical Sciences, Tehran, Iran
3- Department of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran, National Institute of Genetics & Biotechnology, Pajouhesh Boulevard, Town of Science & Technology Research, 15 Kilometer, Highway Tehran- Karaj, Tehran, Iran. Postal Code: 1497716316 ,
Abstract: (10158 Views)
Introduction: Growth hormone is a non-glycosylated polypeptide strand of the pituitary glands of all vertebrates that has a wide range of biological activities and considering the importance of this hormone and its importance and diverse therapeutic applications in medicine, its recombinant production can be of great importance. In recent decades, protein engineering and genetic engineering have resulted in a high level of expression and production of this protein in a variety of hosts, including Escherichia coli bacteria using new techniques and methodes, hormone purification and assay are carried out easily. Therefore, the aim of this review was to investigate the production of recombinant human growth hormone (rhGH) and future challenges.
Conclusion: One of the problems of the expression and purification of the human growth hormone may involve that maybe noted the production of inclusion bodies in the expression of recombinant proteins in the cell cytoplasm, the contamination caused by host proteins, low protein recovery from these inclusion bodies, low protein secretion into the Periplasmic space, high cost of production, especially in Purification stage and so on. Due to the lack of need for glycosylated hormone and high efficiency and simplicity of work, bacterial systems, especially Escherichia coli, are the most economical and effective systems for the expression of heterologous proteins. The hormone purification stage is usually the most costly process. Therefore, an optimal design for achieving the highest target protein recovery with the elimination of all contamination from the final product and reducing the purification step is required.
Conclusion: One of the problems of the expression and purification of the human growth hormone may involve that maybe noted the production of inclusion bodies in the expression of recombinant proteins in the cell cytoplasm, the contamination caused by host proteins, low protein recovery from these inclusion bodies, low protein secretion into the Periplasmic space, high cost of production, especially in Purification stage and so on. Due to the lack of need for glycosylated hormone and high efficiency and simplicity of work, bacterial systems, especially Escherichia coli, are the most economical and effective systems for the expression of heterologous proteins. The hormone purification stage is usually the most costly process. Therefore, an optimal design for achieving the highest target protein recovery with the elimination of all contamination from the final product and reducing the purification step is required.
Keywords: Growth Hormone, Polypeptide, Pituitary Gland, Recombinant Drug, Genetic Engineering, Escherichia coli
Article Type: Review |
Subject:
Agricultural Biotechnology
Received: 2016/04/25 | Accepted: 2017/10/27 | Published: 2018/05/22
Received: 2016/04/25 | Accepted: 2017/10/27 | Published: 2018/05/22
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