目的研究巴罗沙星与 DNA 的分子作用机制和 Mg^(2+)对巴罗沙星与 DNA 相互作用的影响。方法利片J荧光光谱研究巴罗沙星与 DNA 的作用强度并计算热力学数据ΔH;利用紫外光谱、黏度测定、竞争实验、与变性 DNA作用的比较等方法确定巴罗沙...目的研究巴罗沙星与 DNA 的分子作用机制和 Mg^(2+)对巴罗沙星与 DNA 相互作用的影响。方法利片J荧光光谱研究巴罗沙星与 DNA 的作用强度并计算热力学数据ΔH;利用紫外光谱、黏度测定、竞争实验、与变性 DNA作用的比较等方法确定巴罗沙星与小牛胸腺 DNA 的相互作用方式;利用荧光光谱考察 Mg^(2+)对巴罗沙星与小牛胸腺DNA 相互作用的影响。结果 DNA 对巴罗沙星的荧光猝灭常数为(5.43±0.07)×10~3L·mol^(-1),ΔH=-8.03 kJ·mol^(-1);Mg^(2+)使巴罗沙星与 DNA 的作用增强。结论巴罗沙星以沟槽键合方式与 DNA 相瓦作用;Mg^(2+)对巴罗沙星与 DNA 的结合有中介作用。展开更多
The glucose isomerase(GI) was a metal activating enzyme It was most activated by Co 2+ and Mg 2+ ,and Mg 2+ was the best activator,whether the glucose or the xylose was the substrate When the glucose was substrate,the...The glucose isomerase(GI) was a metal activating enzyme It was most activated by Co 2+ and Mg 2+ ,and Mg 2+ was the best activator,whether the glucose or the xylose was the substrate When the glucose was substrate,the dissociation constant of Mg 2+ GI,Co 2+ GI and Mn 2+ -GI was 115 μmol/L,40 μmol/L, and 15 μmol/L respectively. The maximum activity of Mg 2+ GI,Co 2- GI and Mn 2+ GI was 100%,85%,and 20% respectively. When the xylose was substrate,the order of dissociation constant and maximum activity of the metal enzymes was the same Ca 2+ was a competitive inhibitor versus Mg 2+ ( K i 7 4 μmol/L)or Co 2+ ( K i 99 μmol/L). Compared with Mg 2+ GI,the K m of Co 2+ GI was more,and the V M of Co 2+ GI less The process of activity recovery from apo GI to metal GI showed that it was slow and of two展开更多
文摘目的研究巴罗沙星与 DNA 的分子作用机制和 Mg^(2+)对巴罗沙星与 DNA 相互作用的影响。方法利片J荧光光谱研究巴罗沙星与 DNA 的作用强度并计算热力学数据ΔH;利用紫外光谱、黏度测定、竞争实验、与变性 DNA作用的比较等方法确定巴罗沙星与小牛胸腺 DNA 的相互作用方式;利用荧光光谱考察 Mg^(2+)对巴罗沙星与小牛胸腺DNA 相互作用的影响。结果 DNA 对巴罗沙星的荧光猝灭常数为(5.43±0.07)×10~3L·mol^(-1),ΔH=-8.03 kJ·mol^(-1);Mg^(2+)使巴罗沙星与 DNA 的作用增强。结论巴罗沙星以沟槽键合方式与 DNA 相瓦作用;Mg^(2+)对巴罗沙星与 DNA 的结合有中介作用。
文摘The glucose isomerase(GI) was a metal activating enzyme It was most activated by Co 2+ and Mg 2+ ,and Mg 2+ was the best activator,whether the glucose or the xylose was the substrate When the glucose was substrate,the dissociation constant of Mg 2+ GI,Co 2+ GI and Mn 2+ -GI was 115 μmol/L,40 μmol/L, and 15 μmol/L respectively. The maximum activity of Mg 2+ GI,Co 2- GI and Mn 2+ GI was 100%,85%,and 20% respectively. When the xylose was substrate,the order of dissociation constant and maximum activity of the metal enzymes was the same Ca 2+ was a competitive inhibitor versus Mg 2+ ( K i 7 4 μmol/L)or Co 2+ ( K i 99 μmol/L). Compared with Mg 2+ GI,the K m of Co 2+ GI was more,and the V M of Co 2+ GI less The process of activity recovery from apo GI to metal GI showed that it was slow and of two
