Inhibition Kinetics and the Aggregation of α-Glucosidase by Different Denaturants
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- Wu, XQ., Xu, H., Yue, H. et al. Protein J (2009) 28: 448. doi:10.1007/s10930-009-9213-0
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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 α-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.
KeywordsAlpha-glucosidase Inactivation kinetics Aggregation Unfolding
Sodium dodecyl sulfate