title: A convenient method for affinity purification of maltose binding protein fusions.
abstract: Maltose binding protein of Escherichia coli is frequently employed as a fusion partner for the biosynthesis of polypeptides and proteins, largely because of the advantage provided by affinity purification of such a fusion. A mixture of cellulose and starch is shown to be a simple and effective alternative to the use of other, more complicated media which are often used for affinity chromatography of maltose binding protein fusions.
authors.affiliation: Department of Chemistry, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
authors.forename: U
authors.initials: U
authors.lastname: Srinivasan
authors.forename: J A
authors.initials: JA
authors.lastname: Bell
mesh_terms: D018528:ATP-Binding Cassette Transporters; D002352:Carrier Proteins / Q000235:genetics*; D002846:Chromatography, Affinity / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D029968:Escherichia coli Proteins; D006863:Hydrogen-Ion Concentration; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; D009994:Osmolar Concentration; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification*
chemical_list: D018528:ATP-Binding Cassette Transporters; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; D011993:Recombinant Fusion Proteins; C461599:maltose transport system, E coli