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Abstract
Cholera toxin (CT) consists of the A-subunit (ACT) and B-subunit (BCT) consisting of 5 identical beta-peptides. The dynamics of denaturation and subsequent renaturation of CT and BCT was investigated by SE HPLC. The denaturation was performed in the 6M urea at different temperature. The decomposition of CT to ACT and BCT and subsequent breaking of BCT to the beta-peptide is clearly seen at CT denaturation. The proteins were denatured completely and rapidly only when heating urea solution up to 50°C. The renaturation performed with the help of dialysis is more effective than that by chromatography. The quantitative correlation pentamer/monomer of renatured BCT is higher than a fresh solved protein. Thus, a shift of the fluorescence maximum of BCTmight be explained by the presence of some denatured BCT in the solution.