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Unfolding and inactivation of Ampullarium crossean beta-glucosidase during denaturation by guanidine hydrochloride

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Unfolding and inactivation of Ampullarium crossean beta-glucosidase during denaturation by guanidine hydrochloride.htm (413bytes)
Date
2003
Author
Chen, QX
陈清西
Zhang, Z
Huang, H
Zhao, FK(Shanghai Institute of Biochemistry, Chinese Academy of Sciences, Shanghai 200031)
Xu, GJ(Shanghai Institute of Biochemistry, Chinese Academy of Sciences, Shanghai 200031)
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  • 生命科学-已发表论文 [5901]
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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. (C) 2002 Published by Elsevier Science Ltd.
Citation
The International Journal of Biochemistry & Cell Biology 35 (2003) 1227–1233
URI
http://dx.doi.org/doi:10.1016/S0014-5793(03)00891-3
https://dspace.xmu.edu.cn/handle/2288/11036

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