Fractionation techniques in a hydro-organic environment. I. Sulfolane as a solvent for hydrophobic proteins
Articolo
Data di Pubblicazione:
1984
Citazione:
Fractionation techniques in a hydro-organic environment. I. Sulfolane as a solvent for hydrophobic proteins / G. Vecchio, P.G. Righetti, M. Zanoni, G. Artoni, E. Gianazza. - In: ANALYTICAL BIOCHEMISTRY. - ISSN 0003-2697. - 137:2(1984), pp. 410-419.
Abstract:
Sulfolane (thiophene, tethrahydro-1,1-dioxide), at concentrations of 4 m or above, is an efficient solubilizing agent for water-isoluble proteins (e.g., zein or globin chains). In comparison with urea, it appears indefinitely stable in aqueous solutions and does not chemically modify proteins upon storage. Moreover, it favors protein structure, i.e., it increases their α-helix content, while urea decreases it. Sulfolane is compatible with electrophoretic techniques (it only slightly reduces polyacrylamide polymerization efficiency and it does not interfere with protein and peptide detection methods) and with chromatographic methods (it has negligible A280 nm). With hydrophilic proteins, sulfolane behaves as a mild denaturant and precipitates them at concentrations between 5 and 7 m.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
electrophoresis; hydrophobic proteins; ion-exchange chromatography; protein denaturation; sulfolane; urea
Elenco autori:
G. Vecchio, P.G. Righetti, M. Zanoni, G. Artoni, E. Gianazza
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