Overexpression in Escherichia coli, purification and characterization of the molecular chaperone HSC70 |
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Authors: | N Benaroudj B Fang F Triniolles C Ghelis MM Ladjimi |
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Affiliation: | Department of Biochemistry and Biotechnology, Royal Institute of Technology, Stockholm, Sweden. |
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Abstract: | Two different tetrapeptides, AlaTrpTrpPro and AlaIleIlePro, were inserted near the C-terminus of the protein ZZT0. The Trp-rich peptide unit strongly increased both the partitioning of ZZT0 into the polyethylene glycol (PEG)-rich phase in a PEG-potassium phosphate aqueous two-phase system and its retention on PEG and propyl hydrophobic interaction chromatographic columns with potassium phosphate as eluent. Both the partitioning and the retention increased with increasing number of Trp-rich peptide units inserted into ZZT0. Insertion of Ile-rich tetrapeptide units affected the partitioning and retention to a much lesser extent. Partition data also indicated a folding of inserted Trp tetrapeptides units, probably to minimize their water contact. |
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