Abstract
A large number of genetic modifications have been employed to facilitate the purification of numerous recombinant proteins. These techniques have been used for both commercial and research purposes and in a variety of different expression systems. This paper will explore the value of this approach as a research tool and focus primarily on two methods. The first method utilizes a metal-chelate fusion and the second an immuno-affinity fusion. These two methods can be successfully employed in virtually any expression system. The resulting purified protein can be used for a variety of research purposes including refolding studies and pre-clinical biology.
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© 1991 Springer Science+Business Media New York
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Sassenfeld, H.M., Deeley, M., Rubero, J., Shriner, J.C., Madani, H. (1991). Genetic Alterations Which Facilitate Protein Purification: Applications in the Biopharmaceutical Industry. In: Kelly, J.W., Baldwin, T.O. (eds) Applications of Enzyme Biotechnology. Industry-University Cooperative Chemistry Program Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9235-5_19
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DOI: https://doi.org/10.1007/978-1-4757-9235-5_19
Publisher Name: Springer, Boston, MA
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