作者: Ying Zhu , Xue-Ying Song , Wen-Hua Zhao , Ying-Xia Zhang
DOI: 10.1007/S10930-005-7643-X
关键词: Bioorganic chemistry 、 Substrate (chemistry) 、 Magnesium ion 、 Inorganic chemistry 、 Thermal 、 Fluorescence 、 Calf-intestinal alkaline phosphatase 、 Alkaline phosphatase 、 Enzyme 、 Chemistry
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.