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In this study, the interaction of ovalbumin with lutein dipalmitate and the effect of ovalbumin on marigold lutein esters extracts were investigated. Lutein dipalmitate quenched the fluorescence of ovalbumin by static quenching. Binding and thermodynamic parameters proved that lutein dipalmitate bound to ovalbumin spontaneously by van der Waals force and hydrogen bond, and the complex stoichiometry was 11. Through three-dimensional fluorescence spectroscopy, Fourier transform infrared spectroscopy and circular dichroism experiments, th
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