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Updated: Jun 21, 2026

Measuring In Vitro ATPase Activity for Enzymatic Characterization
Published on: August 23, 2016
Characterization of ATPase activity of class II chaperonin from the hyperthermophilic archaeon Pyrococcus furiosus
Hua-you Chen1, Xiao-li Tan, Jian Lu
1Institute for Biological Sciences, Jiangsu University, Zhenjiang, Jiangsu, 212013, China. hyc@ujs.edu.cn
Abstract:
To understand how molecular damage under harsh environmental conditions can be controlled, we investigated the properties of ATPase activity of the chaperonin molecular machinery from the hyperthermophilic archaeon Pyrococcus furiosus (PfCPN). PfCPN ATPase activity depended on K(+) and Mg(2+) and its optimal pH was 7.5. PfCPN had almost no ADPase activity. ADP strongly competitively inhibited PfCPN ATPase activity. Inhibition of PfCPN ATPase decreased its chaperonin activity in protecting lysozyme from heat-induced inactivation.
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