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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleInteraction of lysozyme with negatively charged flexible chain polymerspt_BR
dc.contributor.authorRomanini, Dpt_BR
dc.contributor.authorBraia, Mpt_BR
dc.contributor.authorAngarten, RGpt_BR
dc.contributor.authorLoh, Wpt_BR
dc.contributor.authorPico, Gpt_BR
unicamp.author.emaildianaromanini@hotmail.compt_BR
unicamp.authorUniv Nacl Rosario, Fac Biochem & Pharmaceut Sci, Bioseperat Lab, Dept Chem Phys,FonCyt,CIUNR, Rosario, Argentina Consejo Nacl Invest Cient & Tecn, Rosario, Argentina Univ Estadual Campinas, Inst Chem, Campinas, SP, Brazilpt_BR
dc.subjectlysozymept_BR
dc.subjectpoly vinyl sulfonatept_BR
dc.subjectpoly acrylic acidpt_BR
dc.subjectprotein-polyelectrolyte complexpt_BR
dc.subject.wosBovine Serum-albuminpt_BR
dc.subject.wosPolyelectrolyte Precipitationpt_BR
dc.subject.wosComplex-formationpt_BR
dc.subject.wosProteinspt_BR
dc.subject.wosPurificationpt_BR
dc.subject.wosCalorimetrypt_BR
dc.subject.wosSeparationpt_BR
dc.description.abstractThe 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.pt
dc.relation.ispartofJournal Of Chromatography B-analytical Technologies In The Biomedical And Life Sciencespt_BR
dc.relation.ispartofabbreviationJ. Chromatogr. Bpt_BR
dc.publisher.cityAmsterdampt_BR
dc.publisher.countryHolandapt_BR
dc.publisherElsevier Science Bvpt_BR
dc.date.issued2007pt_BR
dc.date.monthofcirculationSEP 15pt_BR
dc.identifier.citationJournal Of Chromatography B-analytical Technologies In The Biomedical And Life Sciences. Elsevier Science Bv, v. 857, n. 1, n. 25, n. 31, 2007.pt_BR
dc.language.isoenpt_BR
dc.description.volume857pt_BR
dc.description.issuenumber1pt_BR
dc.description.firstpage25pt_BR
dc.description.lastpage31pt_BR
dc.rightsfechadopt_BR
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policypt_BR
dc.sourceWeb of Sciencept_BR
dc.identifier.issn1570-0232pt_BR
dc.identifier.wosidWOS:000249874400004pt_BR
dc.identifier.doi10.1016/j.jchromb.2007.06.025pt_BR
dc.date.available2014-11-20T03:05:43Z
dc.date.available2015-11-26T16:04:10Z-
dc.date.accessioned2014-11-20T03:05:43Z
dc.date.accessioned2015-11-26T16:04:10Z-
dc.description.provenanceMade available in DSpace on 2014-11-20T03:05:43Z (GMT). No. of bitstreams: 1 WOS000249874400004.pdf: 197435 bytes, checksum: 94a2691a1ed77b2654e1a3035f9d2904 (MD5) Previous issue date: 2007en
dc.description.provenanceMade available in DSpace on 2015-11-26T16:04:10Z (GMT). No. of bitstreams: 2 WOS000249874400004.pdf: 197435 bytes, checksum: 94a2691a1ed77b2654e1a3035f9d2904 (MD5) WOS000249874400004.pdf.txt: 29481 bytes, checksum: 182295b72fd3932fbbdb937fd5dd1c34 (MD5) Previous issue date: 2007en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/60369pt_BR
dc.identifier.urihttp://www.repositorio.unicamp.br/handle/REPOSIP/60369
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/60369-
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