Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/60369
Type: Artigo de periódico
Title: Interaction of lysozyme with negatively charged flexible chain polymers
Author: Romanini, D
Braia, M
Angarten, RG
Loh, W
Pico, G
Abstract: 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.
Subject: lysozyme
poly vinyl sulfonate
poly acrylic acid
protein-polyelectrolyte complex
Country: Holanda
Editor: Elsevier Science Bv
Rights: fechado
Identifier DOI: 10.1016/j.jchromb.2007.06.025
Date Issue: 2007
Appears in Collections:Unicamp - Artigos e Outros Documentos

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