Interaction of lysozyme with negatively charged flexible chain polymers

被引:49
作者
Romanini, Diana
Braia, Mauricio
Angarten, Rodrigo Giatte
Loh, Watson
Pico, Guillermo
机构
[1] Natl Univ Rosario, Fac Biochem & Pharmaceut Sci, Bioseperat Lab, Dept Chem Phys,FonCyt,CIUNR, Rosario, Argentina
[2] Consejo Nacl Invest Cient & Tecn, Rosario, Argentina
[3] Univ Estadual Campinas, Inst Chem, Campinas, SP, Brazil
来源
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2007年 / 857卷 / 01期
关键词
lysozyme; poly vinyl sulfonate; poly acrylic acid; protein-polyelectrolyte complex;
D O I
10.1016/j.jchromb.2007.06.025
中图分类号
Q5 [生物化学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
The complex formation between the basic protein lysozyme and anionic polyelectrolytes: poly acrylic acid and poly vinyl sulfonic acid was studied by turbidimetric and isothermal calorimetric titrations. The thermodynamic stability of the protein in the presence of these polymers was also studied by differential scanning calorimetry. The lysozyme-polymer complex was insoluble at pH lower than 6, with a stoichiometric ratio (polymer per protein mol) of 0.025-0.060 for lysozyme-poly vinyl sulfonic acid and around 0.003-0.001 for the lysozyme-poly acrylic acid. NaCl 0.1 M inhibited the complex precipitation in agreement with the proposed coulombic mechanism of complex formation. Enthalpic and entropic changes associated to the complex formation showed highly negative values in accordance with a coulombic interaction mechanism. The protein tertiary structure and its thermodynamic stability were not affected by the presence of polyclectrolyte. (c) 2007 Elsevier B.V. All rights reserved.
引用
收藏
页码:25 / 31
页数:7
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