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The gene coding for human interleukin-5 was synthesized and expressed in Escherichia coli under control of a heat-inducible promoter. High-level expression, 10-15% of total cellular protein, was achieved in E. coli. The protein was produced in an insoluble state. A simple extraction, renaturation and purification scheme is described. The recombinant protein was found to be a homodimer, similar to the natural murine-derived protein. Despite the lack of glycosylation, high specific activities were obtained in three 'in vitro' biological assays. Physical characterization of the protein showed it to be mostly alpha-helical, supporting the hypothesis that a conformational similarity exists among certain cytokines.
A E Proudfoot, and
D Fattah, and
E H Kawashima, and
A Bernard, and
P T Wingfield
April 2006,
Journal of biotechnology,
A E Proudfoot, and
D Fattah, and
E H Kawashima, and
A Bernard, and
P T Wingfield
November 1986,
European journal of biochemistry,
A E Proudfoot, and
D Fattah, and
E H Kawashima, and
A Bernard, and
P T Wingfield
February 2000,
Japanese journal of pharmacology,
A E Proudfoot, and
D Fattah, and
E H Kawashima, and
A Bernard, and
P T Wingfield
April 2010,
Biotechnology and applied biochemistry,
A E Proudfoot, and
D Fattah, and
E H Kawashima, and
A Bernard, and
P T Wingfield
July 2005,
Biotechnology letters,
A E Proudfoot, and
D Fattah, and
E H Kawashima, and
A Bernard, and
P T Wingfield
June 1995,
Biotechnology and applied biochemistry,
A E Proudfoot, and
D Fattah, and
E H Kawashima, and
A Bernard, and
P T Wingfield
April 2005,
Biochimica et biophysica acta,
A E Proudfoot, and
D Fattah, and
E H Kawashima, and
A Bernard, and
P T Wingfield
September 1992,
The Biochemical journal,
A E Proudfoot, and
D Fattah, and
E H Kawashima, and
A Bernard, and
P T Wingfield
June 2007,
Protein expression and purification,
A E Proudfoot, and
D Fattah, and
E H Kawashima, and
A Bernard, and
P T Wingfield
July 1985,
Biochemical and biophysical research communications,
