caa a22 4500 475744071 CHVBK 20180406123508.0 cr unu---uuuuu 170329e20001001xx s 000 0 eng 10.1023/A:1007142117037 doi (NATIONALLICENCE)springer-10.1023/A:1007142117037 Effects of Zinc on Creatine Kinase: Activity Changes, Conformational Changes, and Aggregation [Elektronische Daten] [Xiaofeng Tong, Xiangang Zeng, Hai-Meng Zhou] The effects of zinc on creatine kinase (CK) are very distinctive compared with other bivalent metal ions. Zinc up to 0.1 mM induced increases in CK activity, accompanied by significant hydrophobic surface exposure and increase in a-helix content of CK. Zinc over 0.1 mM denatured and inactived CK. In the presence of 0.1 mM zinc, the CK activity was very close to that of the native CK, but its conformation changed greatly. The kinetic courses of CK inactivation and conformational change in the presence of 1 mM zinc were measured to determine apparent rate constants of inactivation and conformational change. Zinc over 0.05 mM induced CK aggregation at 37°C, and the aggregation was dependent on zinc concentration, CK concentration, and temperature. The inactivation and aggregation can be reversed by EDTA. An explanation for CK aggregation induced by zinc is proposed, as well as a mechanism for CK abnormality in Alzheimer's disease. Plenum Publishing Corporation, 2000 Creatine kinase nationallicence zinc nationallicence activation and inactivation nationallicence conformational change nationallicence aggregation nationallicence Alzheimer's disease nationallicence Tong Xiaofeng Department of Biological Science and Biotechnology, School of Life Science and Engineering, Tsinghua University, 100084, Beijing, China aut Zeng Xiangang Department of Chemical Engineering, Wuyi University, Jiangmen, 529020, Guangdong, China aut Zhou Hai-Meng Department of Biological Science and Biotechnology, School of Life Science and Engineering, Tsinghua University, 100084, Beijing, China aut Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/7(2000-10-01), 553-562 0277-8033 19:7<553 2000 19 10930 https://doi.org/10.1023/A:1007142117037 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1007142117037 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Tong Xiaofeng Department of Biological Science and Biotechnology, School of Life Science and Engineering, Tsinghua University, 100084, Beijing, China aut NATIONALLICENCE 700 1- Zeng Xiangang Department of Chemical Engineering, Wuyi University, Jiangmen, 529020, Guangdong, China aut NATIONALLICENCE 700 1- Zhou Hai-Meng Department of Biological Science and Biotechnology, School of Life Science and Engineering, Tsinghua University, 100084, Beijing, China aut NATIONALLICENCE 773 0- Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/7(2000-10-01), 553-562 0277-8033 19:7<553 2000 19 10930 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer