Structural changes in human serum albumin according to the data on the phosphorescence kinetics of a luminescent probe - Eosin

被引：3
|
作者：
Saletskii A.M. [1 ]
Mel'nikov A.G. [2 ]
Pravdin A.B. [2 ]
Kochubei V.I. [2 ]
Mel'nikov G.V. [3 ]
机构：
[1] M. V. Lomonosov Moscow State University, Moscow
[2] Saratov State University, Saratov
[3] Saratov State Technical University, Saratov, 410057
来源：
Journal of Applied Spectroscopy | 2005年 / 72卷 / 5期
关键词：
Human serum albumin; Luminescent probe; Micelle; Phosphorescence at room temperature; Protein; Protein denaturation; Sodium dodecyl sulfate; Surface-active substance;
D O I：
10.1007/s10812-005-0139-9
中图分类号：
学科分类号：
摘要：
The influence of the human serum albumin (HSA) denaturation by a surface-active substance (sodium dodecyl sulfate (SDS)) on the phosphorescence of a luminescent probe (eosin) has been investigated. The dependences of the eosin-phosphorescence intensity on the SDS concentration were determined at different pH levels of an HSA solution. It has been shown that at SDS concentrations lower than the critical concentration necessary for micelle formation, the hydrophobic interactions of eosin with the protein influence the deactivation of the eosin triplet states. ©2005 Springer Science+Business Media, Inc.
引用
收藏
页码：723 / 727
页数：4
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