Purification of proteins fused to maltose-binding protein

Methods Mol Biol. 2011:681:281-93. doi: 10.1007/978-1-60761-913-0_15.

Abstract

Maltose-binding protein (MBP) is one of the most popular fusion partners being used for producing recombinant proteins in bacterial cells. MBP allows one to use a simple capture affinity step on amylose-agarose columns, resulting in a protein that is often 70-90% pure. In addition to protein-isolation applications, MBP provides a high degree of translation and facilitates the proper folding and solubility of the target protein. This chapter describes efficient procedures for isolating highly purified MBP-target proteins. Special attention is given to considerations for downstream applications such as structural determination studies, protein activity assays, and assessing the chemical characteristics of the target protein.

MeSH terms

  • Amylose / chemistry
  • Chemical Fractionation / instrumentation
  • Chemical Fractionation / methods*
  • Chromatography, Affinity
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Equipment Reuse
  • Escherichia coli / cytology
  • Escherichia coli / genetics
  • Maltose-Binding Proteins / genetics*
  • Protein Engineering / methods*
  • Recombinant Fusion Proteins / genetics*
  • Recombinant Fusion Proteins / isolation & purification*
  • Sepharose / chemistry

Substances

  • Maltose-Binding Proteins
  • Recombinant Fusion Proteins
  • Amylose
  • Sepharose