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Dilute guanidine hydrochloride(cas 50-01-1)

To investigate the changes of vitality and conformation during the renaturation of alkaline phosphatase in human placenta, and to explore its folding mechanism.

MATERIALS AND METHODS: The activity of refolding enzymes was determined by spectrophotometry. The fluorescence spectra were detected by fluorescence method.

Results: The corrective conditions were as follows: guanidine dilution concentration 0.5 mol /L, temperature 4 ℃, refolding solution pH 9.0, time 24 hours. Under these conditions, the enzyme activity and endogenous fluorescence spectra of different concentrations of guanidine hydrochloride(cas 50-01-1) denatured enzyme showed that the enzyme activity and endogenous fluorescence spectra of the degenerated intermediate state were restored to natural state, and the denatured enzyme could only be partially recovered, and with the increase of guanidine concentration, the recovery was more difficult. When the guanidine concentration was 6.0 mol /L, the enzyme activity and endogenous fluorescence spectrum of the denatured enzyme could not be recovered at all.

Conclusion: The degenerated intermediate state enzyme can be completely renatured, while the mutant enzyme is only partially renatured and is related to refolding conditions.



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