大连工业大学学报2012，Vol.31Issue(2)：95-97,3.
丹酚酸A对牛血清白蛋白的荧光猝灭作用
Fluorescence quench to bovine serum albumin by Sal A
张曦 1寇自农 2石羽佳 1朱靖博1
作者信息
- 1. 大连工业大学食品学院,辽宁大连 116034
- 2. 大连工业大学分析测试中心,辽宁大连 116034
- 折叠
摘要
Abstract
The interaction between salvianolic acid A (Sal A) and bovine serum albumin (BSA) at pH 7. 40 was studied by fluorescence spectroscopy. The fluorescence of BSA is quenched obviously by Sal A, the mechanism of fluorescence quench was deemed as static mode. The fluorescence quenching data were analyzed according to Stern-Volmer equation and Lineweaver-Burk equation. The binding constants of Sal A with BSA are obtained at 25, 30, 35 ℃ were 1. 49 × 105, 1. 19 × 105, 8. 24 × 104 L/mol. The thermodynamic parameters, enthalpy change(AH) was calculated to be -56.55 kJ/mol. The results indicated that Sal A could bind with BSA strongly at molar ratio 1 : 1. The hydrophobic interaction force and Van der Waals force play a main role in the binding of Sal A with BSA.关键词
丹酚酸A/牛血清白蛋白/荧光光谱Key words
salvianolic acid A/ BSA/ fluorescence spectroscopy分类
化学化工引用本文复制引用
张曦,寇自农,石羽佳,朱靖博..丹酚酸A对牛血清白蛋白的荧光猝灭作用[J].大连工业大学学报,2012,31(2):95-97,3.
