Su-Fang Wang, Yue-Xiu Si, Zhi-Jiang Wang, Shang-Jun Yin, Jun-Mo Yang, Guo-Ying Qian
College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, PR China.
International journal of biological macromolecules 2012 May 1A folding study of creatine kinase from Pelodiscus sinensis has not yet been reported. To gain more insight into structural and folding mechanisms of P. sinensis CK (PSCK), denaturants such as SDS, guanidine HCl, and urea were applied in this study. We purified PSCK from the muscle of P. sinensis and conducted inhibition kinetics with structural unfolding studies under various conditions. The results revealed that PSCK was completely inactivated at 1.8 mM SDS, 1.05 M guanidine HCl, and 7.5 M urea. The kinetics via time-interval measurements showed that the inactivation by SDS, guanidine HCl, and urea were all first-order reactions with kinetic processes shifting from monophase to biphase at increasing concentrations. With respect to tertiary structural changes, PSCK was unfolded in different ways; SDS increased the hydrophobicity but retained the most tertiary structural conformation, while guanidine HCl and urea induced conspicuous changes in tertiary structures and initiated kinetic unfolding mechanisms. Our study provides information regarding PSCK and enhances our knowledge of the reptile-derived enzyme folding. Copyright © 2012 Elsevier B.V. All rights reserved.
Su-Fang Wang, Yue-Xiu Si, Zhi-Jiang Wang, Shang-Jun Yin, Jun-Mo Yang, Guo-Ying Qian. Folding studies on muscle type of creatine kinase from Pelodiscus sinensis. International journal of biological macromolecules. 2012 May 1;50(4):981-90
PMID: 22405779
View Full Text