Complexation of serum albumins and triton X-100: Quenching of tryptophan fluorescence and analysis of the rotational diffusion of complexes

被引：7

作者：

Vlasova, I. M. ^{[1
,2
]}

Vlasov, A. A. ^{[1
]}

Saletskii, A. M. ^{[1
]}

机构：

[1] Moscow MV Lomonosov State Univ, Fac Phys, Moscow 119991, Russia

[2] Russian Acad Sci, Ctr Theoret Problems Physicochem Pharmacol, Moscow 119991, Russia

来源：

RUSSIAN JOURNAL OF PHYSICAL CHEMISTRY A | 2016年 / 90卷 / 07期

关键词：

bovine serum albumin; human serum albumin; Triton X-100; fluorescence quenching; rotational diffusion; CETYLTRIMETHYLAMMONIUM BROMIDE; INTRINSIC FLUORESCENCE; DENATURATION; PROTEIN;

D O I：

10.1134/S0036024416070335

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The polarized and nonpolarized fluorescence of bovine serum albumin and human serum albumin in Triton X-100 solutions is studied at different pH values. Analysis of the constants of fluorescence quenching for BSA and HSA after adding Triton X-100 and the hydrodynamic radii of BSA/HSA-detergent complexes show that the most effective complexation between both serum albumins and Triton X-100 occurs at pH 5.0, which lies near the isoelectric points of the proteins. Complexation between albumin and Triton X-100 affects the fluorescence of the Trp-214 residing in the hydrophobic pockets of both BSA and HSA.

引用

页码：1479 / 1483

页数：5

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