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Simple Two-step Chromatographic Method for Purification of Ovomacroglobulin
Corresponding Author(s) : Mei-Hu Ma
Asian Journal of Chemistry,
Vol. 25 No. 5 (2013): Vol 25 Issue 5
Abstract
Ovomacroglobulin, also known as ovostatin, has been demonstrated to possess broad-spectrum inhibitory activity against various types of proteases and some other important biological activities, such as inhibiting sepsis, accelerate wound healing and antiinflammatory. In this study, an improved method was developed to purify ovomacroglobulin. Ovomacroglobulin-rich part obtained from polyethylene glycol precipitation (4-8 %) was separated by using Q Sepharose Fast Flow anion-exchange chromatography and then Sephacryl S-200 was employed to the purification of ovomacroglobulin. The recovery of the whole process was 37.76 %, the obtained protein was identified as ovostatin/ovomacroglobulin (Gallus gallus) by LC-ESI-LTQ. This procedure has an advantage in rapid preparation of ovomacroglobulin with a higher recovery.
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- H. Lineweaver and C.W. Murray, J. Biol. Chem., 171, 565 (1947).
- I. Matsushima, Science, 127, 1178 (1958).
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References
H. Lineweaver and C.W. Murray, J. Biol. Chem., 171, 565 (1947).
I. Matsushima, Science, 127, 1178 (1958).
T. Kitamoto, M. Nakashima and A. Ikai, J. Biochem., 92, 1679 (1982).
I. Saxena and S. Tayyab, Cellul, Mol, Life Sci,, 53, 13 (1997).
H. Nagase and E.D. Harris Jr., J. Biol. Chem., 258, 7490 (1983).
H. Nagase, E.D. Harris Jr., J.F. Woessner Jr. and K. Brew, J. Biol. Chem., 258, 7481 (1983).
S. Miyagawa, R. Kamata, K. Matsumoto, R. Okamura and H. Maeda, Graefe's Archive for Clinical and Experimental Ophthalmology, 232, 488 (1994).
K. Maruo, T. Akaike, T. Ono and H. Maeda, Infect. Immun., 66, 866 (1998).
A. Ikai, M. Nakashima and Y. Aoki, Biochem. Biophys. Res. Commun., 158, 831 (1989).
Y. Ofuji, T. Suzuki, H. Yoshie, K. Hara and M. Adachi, Periodontal Clinical Investigations: Official Publication of the Northeastern Society of Periodontists, 14, 13 (1992).
S. Miyagawa, R. Kamata, K. Matsumoto, R. Okamura and H. Maeda, Graefe's Archive for Clinical and Experimental Ophthalmology, 229, 281 (1991).
A. Molla, T. Yamamoto, T. Akaike, S. Miyoshi and H. Maeda, J. Biol. Chem., 264, 10589 (1989).
J.J. Enghild, G. Salvesen, K. Brew and H. Nagase, J. Biol. Chem., 264, 8779 (1989).
K.L. Nielsen, L. Sottrup-Jensen, H. Nagase, H.C. Thogersen and M. Etzerodt, DNA Sequence: The Journal of DNA Sequencing and Mapping, 5, 111 (1994).
N.A. Zorin, V.N. Zorina and R.M. Zorina, J. Evolut. Biochem. Physiol.,42, 112 (2006).
Y. Mine, Egg Bioscience and Biotechnology, Wiley Online Library, (2008).
D. Pinto, E.A. Arriaga, R.M. Schoenherr, S.S.H. Chou and N.J. Dovichi, J. Chromatogr. B, 793, 107 (2003).
D.A. Omana, J. Wang and J. Wu, J. Chromatogr. B, 878, 1771 (2010).
A. Tankrathok, S. Daduang, R. Patramanon, T. Araki and S. Thammasirirak, Prep. Biochem. Biotechnol., 39, 380 (2009).
Y. Guo, Protein Electrophoresis Technology, Science Press, Beijing, (1999).
R. Huopalahti, Bioactive Egg Compounds, Springer Verlag (2007).
X. Zhang, N. Qiu, F. Geng and M. Ma, J. Sep. Sci., 34, 3295 (2011).
R. Bhat and S.N. Timasheff, Protein Sci., 1, 1133 (1992).
K.C. Ingham, Methods Enzymol., 182, 301 (1990).
G. Bassani, B. Farruggia, B. Nerli, D. Rornanini and G. Pico, J. Chromatogr. B, 859, 222 (2007).
Y. Shibusawa, N. Takeuchi, K. Sugawara, A. Yanagida, H. Shindo and Y. Ito, J. Chromatogr. B, 844, 217 (2006).
V. Kumar, V.K. Sharma and D.S. Kalonia, Int. J. Pharmaceut., 366, 38 (2009).
D.H. Atha and K.C. Ingham, J. Biol. Chem., 256, 12108 (1981).
W. Honig and M.R. Kula, Anal. Biochem., 72, 502 (1976).
J. Hirose, Y. Doi, N. Kitabatake and H. Narita, Biosci. Biotechnol. Biochem., 70, 144 (2006).
C. Guerin-Dubiard, M. Pasco, A. Hietanen, A.Q. del Bosque, F. Nau and T. Croguennec, J. Chromatogr. A, 1090, 58 (2005).
F. Nau, M. Pasco, C. Desert, D. Molle, T. Croguennec and C. Guérin Dubiard, J. Agric. Food Chem., 53, 2158 (2005).