Document Type
Book Chapter
Rights
This item is available under a Creative Commons License for non-commercial use only
Disciplines
1.4 CHEMICAL SCIENCES, 1.6 BIOLOGICAL SCIENCES
Abstract
Differential protein precipitation is a rapid and economical step in protein purification and is based on exploiting the inherent physico-chemical properties of the polypeptide. Precipitation of recombinant proteins, lysed from the host cell, is commonly used to concentrate the protein of choice before further polishing steps with more selective purification columns (e.g. His-Tag, Size Exclusion etc.). Recombinant proteins can also precipitate naturally as inclusion bodies due to various influences during over-expression in the host cell. Although this phenomenon permits easier initial separation from native proteins, these inclusion bodies must carefully be differentially solubilised so as to reform functional, correctly folded proteins. Here, a typical protein extraction, precipitation and selective resolubilisation procedure is outlined, based on a recombinantly expressed protein.
DOI
https://doi.org/ 10.1007/978-1-60761-913-0_11
Recommended Citation
Ryan, B.J. (2011). Differential precipitation and solubilization of proteins. Methods in Molecular Biology (Eds. Loughran, S.T. and Walls, D.) Springer Protocols/Humana Press, NY, USA, pp. 203-213. doi:10.1007/978-1-60761-913-0_11
Included in
Biochemistry Commons, Biotechnology Commons, Food Science Commons, Molecular Biology Commons
Publication Details
Ryan, B.J. (2011). Differential precipitation and solubilization of proteins. IN Methods in Molecular Biology (Eds. Loughran, S.T. and Walls, D.) Springer Protocols/Humana Press, NY, USA, pp. 203-213.