光譜法研究三磷酸腺苷二鈉與牛血清白蛋白的相互作用及共存金屬離子的影響
發(fā)布時間:2018-07-21 09:03
【摘要】:在模擬人體生理條件下,用紫外-可見吸收光譜法和熒光光譜法研究三磷酸腺苷二鈉(ADT)和牛血清白蛋白(BSA)的相互作用及共存金屬離子Mn~(~(2+)),Co~(2+),Cr~(3+),Mg~(2+),Fe~(3+)對兩者結(jié)合作用的影響.結(jié)果表明:ADT對BSA的熒光有猝滅作用,其猝滅過程屬于動態(tài)猝滅.通過計算得出ADT與BSA的結(jié)合常數(shù)Kb及結(jié)合為點數(shù)n.根據(jù)熱力學(xué)參數(shù)確定了ADT和BSA之間的作用力類型主要為靜電引力.ADT在BSA中的結(jié)合位點主要位于亞螺旋域ⅡA.Hill系數(shù)nHill≈1,表明ADT對兩者的結(jié)合幾乎無協(xié)同作用.用同步熒光光譜法研究了ADT對BSA構(gòu)象的影響.此外還詳細(xì)探討了共存金屬離子對ADT與BSA結(jié)合作用的影響.
[Abstract]:The interaction of adenosine triphosphate disodium (ADT) with bovine serum albumin (BSA) and the effect of coexisting metal ions mn ~ (2) C ~ (2) C _ (2) C _ (2) mg ~ (2) Fe ~ (3) on the interaction between ADT and bovine serum albumin (BSA) were studied by UV-Vis absorption spectroscopy and fluorescence spectroscopy under simulated human physiological conditions. The results show that the fluorescence of BSA is quenched by: 1. The quenching process is dynamic. The binding constant of ADT and BSA was calculated, and the binding point was n. According to the thermodynamic parameters, the interaction force between ADT and BSA is mainly composed of electrostatic force. The binding site of ADT in BSA is mainly located in the subhelical region 鈪,
本文編號:2135019
[Abstract]:The interaction of adenosine triphosphate disodium (ADT) with bovine serum albumin (BSA) and the effect of coexisting metal ions mn ~ (2) C ~ (2) C _ (2) C _ (2) mg ~ (2) Fe ~ (3) on the interaction between ADT and bovine serum albumin (BSA) were studied by UV-Vis absorption spectroscopy and fluorescence spectroscopy under simulated human physiological conditions. The results show that the fluorescence of BSA is quenched by: 1. The quenching process is dynamic. The binding constant of ADT and BSA was calculated, and the binding point was n. According to the thermodynamic parameters, the interaction force between ADT and BSA is mainly composed of electrostatic force. The binding site of ADT in BSA is mainly located in the subhelical region 鈪,
本文編號:2135019
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