Thermal Inactivation and Unfolding of a Dimeric Arginine Kinase

Title: Thermal Inactivation and Unfolding of a Dimeric Arginine Kinase

Volume: 12 Issue: 4

Author(s): Guo Qin and Wang Xicheng

Affiliation:

Keywords: arginine kinase, thermal denaturation, inactivation, mg, unfolding, fluorescence, fast performance liquid chromatography, differential scanning calorimetry

Abstract: 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°C, a model is suggested for the thermal unfolding of this dimeric AK. In addition, the effect of free Mg2+ and the potential biological significance on the thermal unfolding of dimeric AK is discussed.

Cite this article as:

Qin Guo and Xicheng Wang, Thermal Inactivation and Unfolding of a Dimeric Arginine Kinase, Protein & Peptide Letters 2005; 12 (4) . https://dx.doi.org/10.2174/0929866053765699

DOI https://dx.doi.org/10.2174/0929866053765699	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305