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Compared inactivation and conformational changes of yeast alcohol dehydrogenase at different concentrations of guanidine hydrochloride(50-01-1)

The unfolding of yeast dehydrogenase in guanidine solution was studied by means of fluorescence emission spectroscopy, circular dichroism spectroscopy, second derivative spectroscopy and UV absorption spectroscopy. The inactivation and conformational changes of yeast alcohol dehydrogenase at different concentrations of guanidine hydrochloride(50-01-1) were compared. The results showed that the inactivation of the enzyme was earlier than that of the conformation. When the conformation had not changed significantly in the low concentration of guanidine solution, the enzyme activity was almost completely lost. From the above results, it can be seen that the active site of the Zn ~ (2+) enzyme containing the auxiliary metal ion is also more flexible than the whole structure of the enzyme molecule.

 

 

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