Nowadays for prevention of botulism syndrome, researchers have tended to use recombinant vaccines. One of these vaccines is a recombinant protein containing 93 amino acids of C-terminal of botulinum neurotoxin type E (rBoNT/E-HCC). In this study, after expression and purification of rBoNT/E-HCC, the effect of different pH on the protein was carried out by Circular dichroism (CD) spectrometry and followed by thermodynamics studies. The main goal was, to find the optimum purification condition for this protein and also to evaluate the possibility of using this protein as an oral vaccine. For this purpose, thermal danaturation of rBoNT/E-HCC was studied at four different pH (2, 5, 7.4, and 9) by CD. Our results indicated that Tm and ∆G° of rBoNT/E-HCC are higher in alkaline pH in comparison with acidic pH. Finally, our results suggest that neutral or alkaline pH as the optimum pH for rBoNT/E-HCC purification.
Rostamian, M., Mousavy, S. J., & Ebrahimi, F. (2013). Thermodynamic Study of Carboxy Terminal of Botulinum Neurotoxin Type E by Circular Dichroism Spectroscopy. Journal of Advanced Defense Science & Technology, 4(1), 31-38.
MLA
M. Rostamian; S. J. Mousavy; F. Ebrahimi. "Thermodynamic Study of Carboxy Terminal of Botulinum Neurotoxin Type E by Circular Dichroism Spectroscopy". Journal of Advanced Defense Science & Technology, 4, 1, 2013, 31-38.
HARVARD
Rostamian, M., Mousavy, S. J., Ebrahimi, F. (2013). 'Thermodynamic Study of Carboxy Terminal of Botulinum Neurotoxin Type E by Circular Dichroism Spectroscopy', Journal of Advanced Defense Science & Technology, 4(1), pp. 31-38.
VANCOUVER
Rostamian, M., Mousavy, S. J., Ebrahimi, F. Thermodynamic Study of Carboxy Terminal of Botulinum Neurotoxin Type E by Circular Dichroism Spectroscopy. Journal of Advanced Defense Science & Technology, 2013; 4(1): 31-38.
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