The Protein Journal

, 28:448

Inhibition Kinetics and the Aggregation of α-Glucosidase by Different Denaturants

  • Xue-Qiang Wu
  • Heng Xu
  • Hui Yue
  • Kai-Quan Liu
  • Xiao-Yun Wang

DOI: 10.1007/s10930-009-9213-0

Cite this article as:
Wu, XQ., Xu, H., Yue, H. et al. Protein J (2009) 28: 448. doi:10.1007/s10930-009-9213-0


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.


Alpha-glucosidase Inactivation kinetics Aggregation Unfolding 





Guanidine hydrochloride


p-Nitrophenyl α-d-glucopyranoside




Sodium dodecyl sulfate

Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  • Xue-Qiang Wu
    • 1
  • Heng Xu
    • 2
    • 4
  • Hui Yue
    • 1
  • Kai-Quan Liu
    • 1
  • Xiao-Yun Wang
    • 1
    • 3
  1. 1.College of Life ScienceShandong Agricultural UniversityShandongPeople’s Republic of China
  2. 2.College of Life ScienceJiaying UniversityGuangdongPeople’s Republic of China
  3. 3.State Key Laboratory of Crop BiologyShandongPeople’s Republic of China
  4. 4.College of Life ScienceZhejiang UniversityZhejiangPeople’s Republic of China

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