Abstract
Affinity chromatography enables the separation and isolation of proteins of interest from complex milieu of biochemicals. Nickel-charged affinity resins and amylose resins are two commonly used matrices for the isolation of proteins with histidine tag (6× His-tag) and maltose binding protein (MBP) tag, respectively. Herein we describe the isolation of the Protruding domain (P-domain) of Norovirus’s major capsid protein, VP1, through a highly efficient batch purification technique. By fusing the P-domain to a 6×His-MBP tag followed by a TEV cleavage site, we can effectively purify the P-domain in three chromatography steps (positive nickel affinity, negative nickel affinity, and negative amylose affinity).
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Salmen, W. (2022). Positive and Negative Affinity Chromatography to Purify Norovirus P-Domain Protein. In: Ayyar, B.V., Arora, S. (eds) Affinity Chromatography. Methods in Molecular Biology, vol 2466. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2176-9_6
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DOI: https://doi.org/10.1007/978-1-0716-2176-9_6
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