Aim and Background: 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.
Material & Methods: 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.
Result:The results show that the purified protein has a molecular weight of 31 kDa and the amount of purified protein is 1 mg.
Conclusion: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.
Type of Study:
Research Article |
Subject:
Cellular and molecular Received: 2020/12/15 | Accepted: 2021/06/20 | Published: 2021/07/1