Author:
Carlsson Magnus L. R.,Kanagarajan Selvaraju,Bülow Leif,Zhu Li-Hua
Abstract
AbstractMyoglobin is a heme-protein in the muscle of vertebrates with important functions in the oxygenation of tissues and as a regulator in nitric oxide signaling. Myoglobin from many species is also an important nutritional source of bioavailable iron. In this study, we have successfully produced human myoglobin in the leaves of Nicotiana benthamiana by transient expression using a viral vector delivered by Agrobacterium tumefaciens. Analyses confirmed that heme was incorporated and the protein was functional, with observed properties consistent with those of native myoglobins. A relatively high degree of purity could be achieved with low cost methods. The results show the high potential of plants as a production platform for heme proteins, a group of proteins of interest for iron nutrition applications and possible future pharmaceutical development.
Publisher
Springer Science and Business Media LLC
Reference47 articles.
1. Wittenberg, B. A. & Wittenberg, J. B. Myoglobin-mediated oxygen delivery to mitochondria of isolated cardiac myocytes. Proc. Natl. Acad. Sci. USA 84, 7503–7507 (1987).
2. Wittenberg, J. B. & Wittenberg, B. A. Myoglobin function reassessed. J. Exp. Biol. 206, 2011–2020 (2003).
3. Kendrew, J. C. et al. Structure of myoglobin: A three-dimensional Fourier synthesis at 2 Å. resolution. Nature 185, 422–427 (1960).
4. Antonini, E. & Brunori, M. Hemoglobin and myoglobin in their reactions with ligands. (North Holland Pub. Co., 1971).
5. Hendgen-Cotta, U., Flögel, U., Kelm, M. & Rassaf, T. Unmasking the Janus face of myoglobin in health and disease. J. Exp. Biol. 213, 2734–2740 (2010).
Cited by
21 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献