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Expression and rapid one-step purification of biologically active His-tagged factor C by Ni(2+) affinity column
Z Birkó1, F Schauwecker, F Pfennig
1Department of Human Genetics, Medical and Health Science Center, University of Debrecen, Hungary.
FEMS Microbiology Letters
|March 27, 2001
Abstract:
Factor C is an unusual extracellular protein capable of inducing cytodifferentiation in certain Streptomyces strains. The protein is produced by Streptomyces griseus 45H at such a low amount that the study of its mode of action was hindered by the shortage of purified protein. We report here the expression of C-terminally hexa-His-tagged factor C in Streptomyces lividans and Escherichia coli. Expression in S. lividans is low while in E. coli it is relatively high, yielding about 5--10 mg of biologically fully active protein per liter culture.