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The effect of albumin in photostabilization of riboflavin: A kinetic study
Journal of Photochemistry and Photobiology A: Chemistry ( IF 4.3 ) Pub Date : 2020-02-28 , DOI: 10.1016/j.jphotochem.2020.112456
Adeel Arsalan , Kiran Qadeer , Syed Abid Ali , Sofia Ahmed , Rafeeq Alam Khan , Muhammad Ali Sheraz , Sidra Hassan , Iqbal Ahmad

This investigation involves a study of the photochemical interaction of riboflavin (RF) and bovine serum albumin (BSA) in aqueous solution and the evaluation of this effect on the photostabilization of RF. RF solution (5 × 10–5 M) were irradiated with visible light in the presence of BSA (4.0–6.0 × 10–5 M) at pH 7.4 (0.005 M, phosphate buffer saline) and the apparent first–order rate constants for the photolysis of RF were found to be in the range of 3.92–9.26 × 10–3 min–1. The rate of RF photolysis is inhibited with an increase in the concentration of BSA. The second–order rate constant for the photochemical interaction of RF and BSA at pH 7.4 is 1.22 M–1 min–1. There is a gradual loss of RF fluorescence with an increase in BSA concentration due to the formation of a non–fluorescent complex between the two molecules. The value of Stern-Volmer quenching constant has been determined as 2.673 × 103 M–1. A two-component spectrometric method with correction for irrelevant absorption caused by BSA components has been used to determine RF and its photoproduct, lumichrome (LC), in photolyzed solutions. The mode of photochemical interaction of RF and BSA has been discussed.



中文翻译:

白蛋白对核黄素光稳定作用的动力学研究

这项研究涉及水溶液中核黄素(RF)和牛血清白蛋白(BSA)的光化学相互作用的研究,以及这种对RF的光稳定作用的评估。在pH 7.4(0.005 M,磷酸盐缓冲液)的BSA(4.0–6.0×10 –5 M)存在下,用可见光照射RF溶液(5×10 –5 M),并且表观一级速率常数为发现RF的光解范围为3.92–9.26×10 –3 min –1。随着BSA浓度的增加,RF光解的速率受到抑制。RF和BSA在pH 7.4下的光化学相互作用的二级速率常数为1.22 M –1  min –1。由于两个分子之间形成了非荧光复合物,因此随着BSA浓度的增加,RF荧光逐渐消失。Stern-Volmer猝灭常数的值确定为2.673×10 3 M –1。校正了BSA组分引起的不相关吸收的两组分光谱法已用于测定光解溶液中的RF及其光产物luchrome(LC)。已经讨论了RF和BSA的光化学相互作用的模式。

更新日期:2020-02-28
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