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1. Visser EJ. A review of calcitonin and its use in the treatment of acute pain. Acute Pain. 2005; 7(4): 185-89. http://dx.doi.org/10.1016/j.acpain.2005.09.003 2. Pharmacopoeia B. British Pharmacopoeia Commission London; the Department of Health. Soc Serv Public Saf. 2013; 1: 719-20. 3. Kim KH, Seong BL. Peptide amidation: Production of peptide hormonesin vivo andin vitro. Biotechnol Bioprocess Eng. 2001; 6(4): 244-51. doi:10.1007/BF02931985 4. Gellissen G. Production of Recombinant Proteins: Novel Microbial and Eukaryotic Expression Systems. 1st ed. New Jersey: Wiley-Blackwell. 2005; pp: 11-34. 5. Ishikawa H, Tamaoki H. Production of human calcitonin in Escherichia coli from multimeric fusion protein. J Ferment Bioeng. 1996; 82(2): 140-44. http://dx.doi.org/10.1016/0922-338X(96)85036-7 6. Ray MV, Van Duyne P, Bertelsen AH, Jackson-Matthews DE, Sturmer AM, Merkler DJ, et al. Production of recombinant salmon calcitonin by in vitro amidation of an Escherichia coli produced precursor peptide. Biotechnology (N Y). 1993 Jan; 11(1): 64-70. 7. Villalobos A, Ness JE, Gustafsson C, Minshull J, Govindarajan S. Gene Designer: a synthetic biology tool for constructing artificial DNA segments. BMC Bioinformatics. 2006 Jun; 7: 285. 8. Sample & Assay Technologies QIAGEN. QIAprep ® Miniprep Handbook For purification of molecular biology grade DNA. May 2012. 9. Salis HM. The ribosome binding site calculator. Methods Enzymol. 2011; 498: 19-42. doi:10.1016/B978-0-12-385120-8.00002-4 10. Arabanian A, Mohammadnejad M, Balalaie S. A novel and efficient approach for the amidation of C-terminal peptides. Journal of the Iranian Chemical Society. 2010 Dec; 7(4): 840-45. doi:10.1007/BF03246077 11. Balbas P, Lorence A. Recombinant gene expression: reviews and protocols. 2nd ed. New York: Humana Press. 2004.
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