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dc.contributor.author
Mazzaferro, Laura  
dc.contributor.author
Breccia, Javier Dario  
dc.contributor.author
Andersson, Maria M.  
dc.contributor.author
Hitzmann, Bernd  
dc.contributor.author
Hatti Kaul, Rajni  
dc.date.available
2019-08-14T14:21:58Z  
dc.date.issued
2010-07  
dc.identifier.citation
Mazzaferro, Laura; Breccia, Javier Dario; Andersson, Maria M.; Hitzmann, Bernd; Hatti Kaul, Rajni; Polyethyleneimine-protein interactions and implications on protein stability; Elsevier Science; International Journal of Biological Macromolecules; 47; 1; 7-2010; 15-20  
dc.identifier.issn
0141-8130  
dc.identifier.uri
http://hdl.handle.net/11336/81594  
dc.description.abstract
Protein stability assessment of seven model proteins in the presence of low molecular weight polyethyleneimine (PEI, MW 2000Da) was performed. Thermodynamic stability, monitored by circular dichroism (CD) spectroscopy, showed that the polymer did not have a major effect on the melting temperature (T m ) of the basic proteins - muscle lactate dehydrogenase (LDH), ribonuclease A, lysozyme and cutinase, while for the acidic ones - human growth hormone, human serum albumin and heart lactate dehydrogenase - there was a shift in T m towards lower temperatures. The secondary structures of the basic proteins were essentially the same, with none or a slight increase in the CD spectra, in presence of the polymer. In the case of the acidic proteins, the CD spectra were diminished mostly due to phase separation. Assuming a homogeneous distribution of the net charge on the protein surface a quantitative inverse relationship was established between surface charge density of the acidic proteins and the PEI 2000 concentration required for maximum flocculation. Despite lowering the thermal stability of acidic proteins, PEI 2000 was seen to protect heart LDH at an increasing oxidative stress.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier Science  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Oxidation  
dc.subject
Polycation  
dc.subject
Thermodynamic Stability  
dc.subject.classification
Físico-Química, Ciencia de los Polímeros, Electroquímica  
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Ciencias Químicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Polyethyleneimine-protein interactions and implications on protein stability  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2019-08-13T19:16:14Z  
dc.journal.volume
47  
dc.journal.number
1  
dc.journal.pagination
15-20  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Amsterdam  
dc.description.fil
Fil: Mazzaferro, Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina  
dc.description.fil
Fil: Breccia, Javier Dario. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Departamento de Química; Argentina  
dc.description.fil
Fil: Andersson, Maria M.. Lund University; Suecia  
dc.description.fil
Fil: Hitzmann, Bernd. Universität Hannover; Alemania  
dc.description.fil
Fil: Hatti Kaul, Rajni. Lund University; Suecia  
dc.journal.title
International Journal of Biological Macromolecules  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141813010001212  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1016/j.ijbiomac.2010.04.003