Effects of magnesium ions on thermal inactivation of alkaline phosphatase.

作者: Ying Zhu , Xue-Ying Song , Wen-Hua Zhao , Ying-Xia Zhang

DOI: 10.1007/S10930-005-7643-X

关键词: Bioorganic chemistrySubstrate (chemistry)Magnesium ionInorganic chemistryThermalFluorescenceCalf-intestinal alkaline phosphataseAlkaline phosphataseEnzymeChemistry

摘要: The effect of Mg2+ on the thermal inactivation and unfolding calf intestinal alkaline phosphatase has been studied at different temperatures concentrations. Increasing concentration in denatured system significantly enhanced enzyme during inactivation. analysis kinetic course substrate reaction showed that 47°C increased free caused rate to increase. temperature strengthened Control experiment this is not due salt effect. time fluorescence emission spectra maximum for Mg2+-containing was always higher than Mg2+-free system, difference. In addition, Mg2+also 47°C. potential biological significance these results are discussed.

参考文章(27)
R H Himes, P R Burton, J M Gaito, Dimethyl sulfoxide-induced self-assembly of tubulin lacking associated proteins. Journal of Biological Chemistry. ,vol. 252, pp. 6222- 6228 ,(1977) , 10.1016/S0021-9258(17)40053-6
Eunice E. Kim, Harold W. Wyckoff, Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis. Journal of Molecular Biology. ,vol. 218, pp. 449- 464 ,(1991) , 10.1016/0022-2836(91)90724-K
D L Hwang, C F Yen, J L Nadler, Insulin increases intracellular magnesium transport in human platelets. The Journal of Clinical Endocrinology and Metabolism. ,vol. 76, pp. 549- 553 ,(1993) , 10.1210/JCEM.76.3.8445010
José Luis Millán, William H. Fishman, R. Stinson, Biology of Human Alkaline Phosphatases with Special Reference to Cancer Critical Reviews in Clinical Laboratory Sciences. ,vol. 32, pp. 1- 39 ,(1995) , 10.3109/10408369509084680
Thomas T. Tibbitts, Jennifer E. Murphy, Evan R. Kantrowitz, Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase. Journal of Molecular Biology. ,vol. 257, pp. 700- 715 ,(1996) , 10.1006/JMBI.1996.0195
Michel Fosset, Danielle Chappelet-Tordo, Michel Lazdunski, Intestinal alkaline phosphatase. Physical properties and quaternary structure. Biochemistry. ,vol. 13, pp. 1783- 1788 ,(1974) , 10.1021/BI00706A001
Marc F. Hoylaerts, Thomas Manes, José Luis Millán, Mammalian Alkaline Phosphatases Are Allosteric Enzymes Journal of Biological Chemistry. ,vol. 272, pp. 22781- 22787 ,(1997) , 10.1074/JBC.272.36.22781
R. A. Anderson, W. F. Bosron, F. S. Kennedy, B. L. Vallee, Role of magnesium in Escherichia coli alkaline phosphatase. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 72, pp. 2989- 2993 ,(1975) , 10.1073/PNAS.72.8.2989