Citrate and Phosphate Influence on Green Fluorescent Protein Thermal Stability

被引：11

作者：

de Lencastre Novaes, Leticia C. ^{[1
]}

Mazzola, Priscila G. ^{[2
]}

Pessoa, Adalberto, Jr. ^{[1
]}

Vessoni Penna, Thereza C. ^{[1
]}

机构：

[1] Univ Sao Paulo, Sch Pharmaceut Sci, Dept Pharmaceut Technol & Biochem, Sao Paulo, SP, Brazil

[2] Univ Estadual Campinas, Fac Med Sci, Dept Clin Pathol, Campinas, SP, Brazil

来源：

BIOTECHNOLOGY PROGRESS | 2011年 / 27卷 / 01期

基金：

巴西圣保罗研究基金会;

关键词：

green fluorescent protein; salt; citrate; phosphate; protein stability; thermal stability; SALT CONCENTRATION; GROWTH-FACTOR; GFP; TEMPERATURE; PH;

D O I：

10.1002/btpr.495

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Protein structure and function can be regulated by no specific interactions, such as ionic interactions in the presence of salts. Green fluorescent protein (GFP) shows remarkable structural stability and high fluorescence; its stability can be directly related to its fluorescence output, among other characteristics. GFP is stable under increasing temperatures, and its thermal denaturation is highly reproducible. The aim of this study was to evaluate the thermal stability of GFP in the presence of different salts at several concentrations and exposed to constant temperatures, in a range of 70-95 degrees C. Thermal stability was expressed in decimal reduction time. It was observed that the D-values obtained were higher in the presence of citrate and phosphate, when compared with that obtained in their absence, indicating that these salts stabilized the protein against thermal denaturation. (C) 2010 American Institute of Chemical Engineers Biotechnol. Prog., 27: 269-272, 2011

引用

页码：269 / 272

页数：4

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