Abstract
The redox system of reduced and oxidized dithiothreitol, DTT(SH) 2/DTT(S-S), was followed in the presence of bovine pancreatic trypsin inhibitor (BPTI) from buffer solution pH 8.8 using differential pulse polarography (DPP). The reduction of -S-S- bonds in protein with DTT(SH) 2 was investigated either in absence or in the presence of denaturant such as guanidine hydrochloride (Gdn-HCl). From the analysis of -SH and -S-S- DPP peak current intensities, the kinetic of BPTI unfolding was estimated. It was found that the reaction rate is one order of magnitude higher when denaturant is present, indicating that the lifetime of the corresponding intermediary is shortened.
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