Thermal inactivation and unfolding of a dimeric arginine kinase.
Thermal inactivation and unfolding of the dimeric arginine kinase (AK) from sea cucumber Stichopus japonicus was investigated. The activation energy was calculated to be 388 kJ/mol. Based on the analysis of the denaturation course at 58 degrees C, a model is suggested for the thermal unfolding of this dimeric AK. In addition, the effect of free Mg(2+) and the potential biological significance on the thermal unfolding of dimeric AK is discussed.
Qin
Guo
G
Department of Biological Science and Biotechnology, School of Life Sciences and Engineering, Tsinghua University, Beijing, China.
Xicheng
Wang
W
D000818:Animals; D001122:Arginine Kinase / Q000737:chemistry*; D002152:Calorimetry, Differential Scanning; D005453:Fluorescence; D008956:Models, Chemical; D011487:Protein Conformation; D011489:Protein Denaturation; D047528:Stichopus / Q000201:enzymology; D013696:Temperature
D001122:Arginine Kinase