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Journal of Biomedicine and Biotechnology
Volume 2011, Article ID 873874, 8 pages
http://dx.doi.org/10.1155/2011/873874
Research Article

Expression of Recombinant Human Coagulation Factor VII by the Lizard Leishmania Expression System

1Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran
2Cellular and Molecular Biology Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran
3Biotechnology Department, Pasteur Institute, Tehran, Iran
4Department of Hematology, Faculty of Paramedical Sciences, Shahid Beheshti University of Medical Sciences, Tehran, Iran
5Biotechnology Department, Faculty of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran

Received 19 March 2011; Revised 28 April 2011; Accepted 17 June 2011

Academic Editor: Michael Kalafatis

Copyright © 2011 Sina Mirzaahmadi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

The variety of recombinant protein expression systems have been developed as a resource of FVII gene expression. In the current study, the authors used a novel protein expression system based on the Iranian Lizard Leishmania, a trypanosomatid protozoan as a host for expression of FVII. Plasmid containing cDNA encoding full-length human FVII was introduced into Lizard Leishmania and positive transfectants were analyzed by SDS-PAGE and Western blot analysis. Furthermore, biological activity of purified protein was detected by PT assay. The recombinant strain harboring a construct was analyzed for expression of FVII at the mRNA and protein level. Purified rFVII was obtained and in order to confirm the purified compound was in fact rFVII. Western blot analysis was carried out. Clotting time in PT assay was reduced about 30 seconds with the purified rFVII. In Conclusion, this study has demonstrated, for the first time, that Leishmania cells can be used as an expression system for producing recombinant FVII.