Solvent properties governing protein partitioning in polymer/polymer aqueous two-phase systems

• Tipo: Artigo em Revista Científica Internacional
• Data: 2011

Autores

Pedro P. Madeira (Autor) FEUP; Celso Reis (Autor) ICBAS; Alírio Rodrigues (Autor) FEUP; Mikheeva, LM (Autor) Outra; Chait, A (Autor) Outra; Zaslavsky, BY (Autor) Outra

Revista

Título: Journal of Chromatography A

Vol. 1218

Páginas: 1379-1384

ISSN: 0021-9673

Editora: Elsevier

Indexação

ISI Web of Knowledge - 49 Citações

Scopus - 51 Citações

Outras Informações

ID Authenticus: P-002-T92

DOI: 10.1016/j.chroma.2011.01.020

Abstract (EN): Distribution coefficients of various proteins were measured in aqueous Dextran-Ficoll, Dextran-PES, and Ficoll-PES two-phase systems, containing 0.15 M NaCl in 0.01 M phosphate buffer, pH 7.4. The acquired data were combined with data for the same proteins in different systems reported previously [29,30] and known solvatochromic solvent properties of the systems [17] to characterize the protein-solvent interactions. The relative susceptibilities of proteins to solvent dipolarity/polarizability, solvent hydrogen bond acidity, solvent hydrogen bond basicity, and solvent ability to participate in ion-ion and ion-dipole interactions were characterized. These parameters, which are representative of solute-solvent interactions, adequately described the partitioning of the proteins in each system. It was found that the relative susceptibilities of proteins to solvent dipolarity/polarizability are interrelated with their relative susceptibilities to solvent hydrogen bond acidity and solvent hydrogen bond basicity similarly to those established previously for small nonionic organic compounds.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 6