Cloning, expression and purification of vibrioblock proteins as candidates for cholera
With the advent of cloning technology and recombinant DNA, it became possible to produce drugs and vaccines that were not possible in the past. Recombinant protein occupies a large part of the biopharmaceutical industry, one of the most important of which is vaccination.
In this study, with the aim of obtaining a protein candidate for cholera vaccine, first cloning of a plasmid designed for the bacterial host E.coli DE3 Rossetagami was transformed, then expression was induced using IPTG and after protein expression was examined by SDS-PAGE gel electrophoresis, and then the protein was purified by nickel-sepharose (NI-NTA) chromatography column.
The results show that the purified protein has a molecular weight of 31 kDa and the amount of purified protein is 1 mg.
Based on previous studies as well as the results of this study, the resulting protein can be considered as a suitable candidate for the cholera vaccine.
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