Efficient refolding of a hydrophobic protein with multiple S–S bonds by on-resin immobilized metal affinity chromatography

Sharapova, Olga A.; Yurkova, Maria S.; Laurinavichyute, Daniela K.; Andronova, S. M.; Федоров, А. Н.; Северин, С Е; Северин, Е. С.

doi:10.1016/j.chroma.2011.05.075

Cited by 11 publications

(1 citation statement)

References 14 publications

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“…The polyhistidine tags with immobilized metal ions can form high-affinity (Li et al 2004). Using a silica-based matrix instead of agarose-based material for IMAC to refold hydrophobic proteins contained multiple disulfide bonds can significantly improve proteins refolding yields (Sharapova et al 2011). One of the limitations of IMAC is that the intended protein use can be affected by metal ion carryover or by the fact that the target protein carries a tag that may require further tag removal and cleanup of the final product.…”

Section: Purification Of Recombinant Proteasesmentioning

confidence: 99%

Approaches for the generation of active papain-like cysteine proteases from inclusion bodies of Escherichia coli

Ling

Zhang

Lin

et al. 2015

World J Microbiol Biotechnol

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Papain-like cysteine proteases are widely expressed, fulfill specific functions in extracellular matrix turnover, antigen presentation and processing events, and may represent viable drug targets for major diseases. In depth and rigorous studies of the potential for these proteins to be targets for drug development require sufficient amounts of protease protein that can be used for both experimental and therapeutic purposes. Escherichia coli was widely used to express papain-like cysteine proteases, but most of those proteases are produced in insoluble inclusion bodies that need solubilizing, refolding, purifying and activating. Refolding is the most critical step in the process of generating active cysteine proteases and the current approaches to refolding include dialysis, dilution and chromatography. Purification is mainly achieved by various column chromatography. Finally, the attained refolded proteases are examined regarding their protease structures and activities.

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Section: Purification Of Recombinant Proteasesmentioning

confidence: 99%

Approaches for the generation of active papain-like cysteine proteases from inclusion bodies of Escherichia coli

Ling

Zhang

Lin

et al. 2015

World J Microbiol Biotechnol

View full text Add to dashboard Cite

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Protein renaturation with simultaneous purification by protein folding liquid chromatography: recent developments

Wang

Geng

2013

Amino Acids

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Protein folding liquid chromatography (PFLC)is a powerful tool for protein refolding with simultaneous purification. We review its recent progress in liquid chromatography and molecular biology, primarily involving the validation of PFLC refolding of proteins containing multiple disulphide bonds, the application of mixed-mode chromatography, PFLC in molecular biology. Representative examples are described.

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Production and on-column re-folding of human vascular endothelial growth factor 165 in Escherichia coli

Bang

Kim

Chang

et al. 2013

Biotechnol Bioproc E

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Efficient refolding of a hydrophobic protein with multiple S–S bonds by on-resin immobilized metal affinity chromatography

Cited by 11 publications

References 14 publications

Approaches for the generation of active papain-like cysteine proteases from inclusion bodies of Escherichia coli

Approaches for the generation of active papain-like cysteine proteases from inclusion bodies of Escherichia coli

Protein renaturation with simultaneous purification by protein folding liquid chromatography: recent developments

Production and on-column re-folding of human vascular endothelial growth factor 165 in Escherichia coli

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