Solid-phase Refolding of Immobilized Enterokinase for Fusion Protein Cleavage
2003
Suh, C.W. | Na, S.J. | Lee, E.K. (Hanyang University, Ansan, Republic of Korea) | Park, S.H. | Park, S.G. (Dae Woon Corp., Yongin, Republic of Korea)
Solid-phase refolding of immobilized proteins can be an effective way to reuse an immobilized enzyme column. Oriented immobilization methods are known to provide higher activity of the immobilized enzymes. In this study, using recombinant EK(enterokinase) as a model enzyme and a fusion protein, that consisted of recombinant human growth hormone and six His tag that was linked by the peptide of EK-specific recognition sequence, as a model substrate, we evaluated two oriented immobilization methods, Ñí. e., reductive alkylation of N-terminus Ñß-amine and affinity interaction between poly-histidine tag and Ni-NtA (nickel-nitrilotriacetic acid).
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