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ECB-ART-39423
Protein Pept Lett 2005 May 01;124:369-73. doi: 10.2174/0929866053765699.
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Thermal inactivation and unfolding of a dimeric arginine kinase.

Qin G , Xicheng W .


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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.

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Genes referenced: LOC100887844