化学
荧光
折叠(DSP实现)
猝灭(荧光)
β-乳球蛋白
视黄醇
生物物理学
荧光光谱法
蛋白质折叠
色谱法
光化学
生物化学
乳清蛋白
维生素
生物
电气工程
物理
量子力学
工程类
作者
Éric Dufour,Gaston Hui Bon Hoa,Tomasz Haertlé
标识
DOI:10.1016/0167-4838(94)90204-6
摘要
The effects of pressure (0.1 MPa to 400 MPa) on intrinsic fluorescence of β-lactoglobulin and on its binding of retinol and cis-parinaric acid have been studied at neutral and acid pHs. In neutral pH, fluorescence emission spectra of β-lactoglobulin tryptophanes are characterized by an irreversible 14 nm red-shift indicating pressure-induced folding changes. The intensity of the fluorescence of retinol in β-lactoglobulin-retinol complex is enhanced by a pressure increase up to 150 MPa. It decreases at higher pressures and disappears altogether at 300 MPa. β-Lactoglobulin-retinol complex does not reassociate after decompression at neutral pH. At acid pH condition, the fluorescence quenching by pressure of β-lactoglobulin tryptophans is coupled with a 2 nm spectral shift and is fully reversible demonstrating almost complete restoration of globulin folding. The evolution of retinol fiuorescence in β-lactoglobulin-retinol complex is also entirely reversible between 0.1 MPa and 400 MPa and the complex never dissociates in the studied pressure range. β-lactoglobulin-cis-parinaric acid complexes at neutral and acid pH values dissociate irreversibly at 200 MPa and 350 MPa, respectively.
科研通智能强力驱动
Strongly Powered by AbleSci AI