Toxic Effects of Ethanol on Bovine Serum Albumin

被引：58

作者：

Liu, Rutao ^{[1
]}

Qin, Pengfei ^{[1
]}

Wang, Li ^{[1
]}

Zhao, Xingchen ^{[1
]}

Liu, Yihong ^{[1
]}

Hao, Xiaopeng ^{[2
]}

机构：

[1] Shandong Univ, Sch Environm Sci & Engn, Jinan 250100, Peoples R China

[2] Shandong Univ, State Key Lab Crystal Mat, Jinan 250100, Peoples R China

来源：

JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY | 2010年 / 24卷 / 01期

关键词：

Bovine Serum Albumin; Ethanol; Protein Denaturation; Toxic Effects; CONFORMATION; PRESSURE; PROTEINS;

D O I：

10.1002/jbt.20314

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The toxic effects of ethanol on bovine serum albumin (BSA) were measured by resonance light scattering (RLS), fluorescence spectroscopy, ultraviolet spectrophotometry (UV), circular dichroism (CD), and transmission electron microscopy (TEM). The results indicated that ethanol had toxic effects on BSA, which led to protein denaturation and the effects increased with the ethanol dose. By means of RLS, BSA was found to aggregate in the presence of ethanol and particles smaller than 100 nm were observed from TEM. The fluorescence spectra showed that the intensity of the characteristic peak of BSA decreased and blue shifted, because of changes in the BSA skeleton structure, as well as alteration of the microenvironment of tryptophan (Trp) residues. The conformation changes of BSA were also shown by UV and CD spectrometry. (C) 2010 Wiley Periodicals, Inc. J Biochem Mol Toxicol 24:66-71, 2010; Published online in Wiley InterScience (www.interscience.wiley.com). DOT 1.0:1002/jbt.20314

引用

页码：66 / 71

页数：6

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