Genetic alterations which facilitate protein purification: applications in the biopharmaceutical industry
1991
Sassenfeld, H.M. | Deeley, M. | Rubero, J. | Shriner, J.C. | Madani, H.
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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