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Effects of guanidine hydrochloride(50-01-1) on endogenous fluorescence and denaturation of Trx-GcGASA

Based on SDS-polyacrylamide gel electrophoresis, the purified homocicked gibberellic acid-rich cysteine-rich protein (Trx-GcGASA) was purified and identified on the basis of steady-state fluorescence spectroscopy. The effects of dithiothreitol (DTT), oxidized glutathione (GSSG), hydrogen peroxide and guanidine hydrochloride(50-01-1) on the endogenous fluorescence and degeneration of Trx-GcGASA were studied.

It was found that (1) the endogenous fluorescence of the fusion protein in the neutral buffer system was dominated by the fluorescence emission of 305 nm tyrosine; (2) the degradation of the tryptophan and tyrosine; (3) After 0.5 mmol.L-1GSSG, 5 mmol.L-1 hydrogen peroxide treatment, the fluorescence intensity of tyrosine and tryptophan decreased by about 12 ~ 21 (P <0.05), and the fluorescence intensity of tyrosine and tryptophan decreased by about 12 ~ 21; (4) whether or not the use of 1 mmol.L-1DTT treatment, 6 mol.L-1 guanidine hydrochloride can not induce complete fusion of fusion protein; (5) the presence of disulfide bonds affect the guanidine hydrochloride induced degeneration process. The Gibbs free energy change ΔG of the Trx-GcGASA denaturation process is about 3.7 kJ.mol-1 by two-state model fitting. The related work not only provides a basis for further study of the effect of fusion partner Trx on GtGASA denaturation thermodynamics, dynamics and renaturation process. At the same time, it provides the basic data for obtaining the structural information of GcGASA by spectral means.

 

 

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