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Protein J. 2009 Dec;28(9-10):448-56. doi: 10.1007/s10930-009-9213-0.

Inhibition kinetics and the aggregation of alpha-glucosidase by different denaturants.

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  • 1College of Life Science, Shandong Agricultural University, 271018 Shandong, Tai'an, People's Republic of China.


Kinetic changes of alpha-glucosidase from Saccharomyces cerevisiae in guanidinium chloride (GdmCl) and SDS solutions were investigated. The results showed both denaturants can lead conformational changes and loss of enzymatic activities. However, the concentrations of denaturants causing loss of activities were much lower than that of conformational changes, which suggested that the conformation of active site of alpha-glucosidase was more fragile than the whole molecular conformation in response to the two denaturants. According to the different kinetic process of the enzyme in the GdmCl and SDS solutions, the further investigation on the process of denaturation were made, it showed GdmCl and SDS had different types of inhibition and different types of interaction with the enzyme. Furthermore, the mechanisms of the two denaturants were discussed.

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