A convenient method for affinity purification of maltose binding protein fusions.
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.
Srinivasan
U
U
Department of Chemistry, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
Bell
J A
JA
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*
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