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

• Type: Article in International Scientific Journal
• Date: 2011

Authors

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

Journal

Title: Journal of Chromatography A

Vol. 1218

Pages: 1379-1384

ISSN: 0021-9673

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 49 Citations

Scopus - 51 Citations

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6