Protein Isolation Using Multipurpose Peptide Tags

August 15, 2008

A research group at Lund University (Lund, Sweden) fused a multifunctional peptide tag to the N-terminal ends of green fluorescent protein, lactate dehydrogenase, and human hemoglobin in preparation for separation via ion-exchange chromatography, immobilized metal-ion affinity chromatography, and hydrophobic interaction chromatography.

A research group at Lund University (Lund, Sweden) fused a multifunctional peptide tag to the N-terminal ends of green fluorescent protein, lactate dehydrogenase, and human hemoglobin in preparation for separation via ion-exchange chromatography, immobilized metal-ion affinity chromatography, and hydrophobic interaction chromatography. The peptide tag consisted of histidine, tyrosine, and aspartate residues. They found the tagged green fluorescent protein to be retained longer in both hydrophobic interaction and ion-exchange chromatography.