Thermal Inactivation and Unfolding of a Dimeric Arginine Kinase

Guo      Qin; Wang      Xicheng

doi:10.2174/0929866053765699

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.

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

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Protein & Peptide Letters

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.

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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