Aggregation of the yellow fluorescent protein zFP538 is pH-dependent

被引：0
|
作者：
Zubova, NN [1 ]
Leonid, MVB [1 ]
Savitsky, AP [1 ]
机构：
[1] Moscow MV Lomonosov State Univ, Fac Chem, Dept Chem Enzymol, Moscow 119899, Russia
来源：
GENETICALLY ENGINEERED AND OPTICAL PROBES FOR BIOMEDICAL APPLICATIONS II | 2004年 / 5329卷
关键词：
yellow fluorescent protein zFP538; aggregation; fluorescence; coral proteins; phycobiliproteins;
D O I：
10.1117/12.531480
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
pH-dependent aggregation and dissociation of yellow fluorescent protein zFP538 were studied by gel-filtration, dynamic light scattering, and fluorescence spectroscopy. According to the gel-filtration data for low concentration of zFP538 the molecular weight of aggregates decreases upon changing pH from alkaline to neutral. Dynamic light scattering showed that zFP538 aggregates strongly in concentrated solutions. Aggregation influences heavily the pH-profile of fluorescence of zFP538 and stabilizes zFP538 against fluorescence quenching on acidification. Reduction of the protein concentration results in the shifting of pH profile to the alkaline region. Conclusion: aggregation of the yellow fluorescent protein zFP538 depends on pH; dilution of the protein solution is accompanied by dissociation of zFP538 aggregates under neutral and alkaline pH.
引用
收藏
页码：187 / 191
页数：5
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