Thermal Inactivation and Unfolding of a Dimeric Arginine Kinase

Guo Qin; Wang Xicheng

doi:10.2174/0929866053765699

ISSN: 0929-8665
E-ISSN: 1875-5305

Thermal Inactivation and Unfolding of a Dimeric Arginine Kinase
Authors: Guo Qin¹ and Wang Xicheng²
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¹ Department of Biological Science and Biotechnology, School of Life Sciences and Engineering, Tsinghua University, Beijing 100084 China. ² Department of Biological Science and Biotechnology, School of Life Sciences and Engineering, Tsinghua University, Beijing 100084 China.
Source: Protein and Peptide Letters, Volume 12, Issue 4, May 2005, p. 369 - 373
DOI: https://doi.org/10.2174/0929866053765699
- Available online: 01 May 2005

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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2005-05-01

2025-10-15

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Article Type: Review Article

Keyword(s): arginine kinase; differential scanning calorimetry; fast performance liquid chromatography; fluorescence; inactivation; mg; thermal denaturation; unfolding

Thermal Inactivation and Unfolding of a Dimeric Arginine Kinase

Abstract

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