Unfolding and inactivation of Ampullarium crossean beta-glucosidase during denaturation by guanidine hydrochloride
Qing-Xi Chen1, Zhe Zhang, Huang Huang
1Department of Biology, School of Life Sciences, Xiamen University, PR China. chenqx@jiangxian.xmu.edu.cn
Abstract:
Changes of activity and conformation of Ampullarium crossean beta-glucosidase in different concentrations of guanidine hydrochloride (GuHCl) have been studied by measuring the fluorescence spectra and its relative activity after denaturation. The fluorescence intensity of the enzyme decreased distinctly with increasing guanidine concentrations, the emission peaks appeared red shifted (from 338.4 to 350.8 nm), whereas a new fluorescence emission peak appeared near 310 nm. Changes in the conformation and catalytic activity of the enzyme were compared. A corresponding rapid decrease in catalytic activity of the enzyme was also observed. The extent of inactivation was greater than that of conformational changes, indicating that the active site of the enzyme is more flexible than the whole enzyme molecule. k(+0)>k(+0)' also showed that the enzyme was protected by substrate to a certain extent during guanidine denaturation.
More Related Videos
10:26Elucidating β-1,3-Glucanase and Peroxidase Physicochemical Properties of Wheat Cell Wall Defense Mechanism Against Diuraphis noxia Infestation
Published on: July 26, 2024
13:35Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
Published on: May 23, 2025
Related Concept Videos
Protein Folding Quality Check in the RER
Protein Denaturation
Activation and Inactivation of G Proteins
GPCR Desensitization
