Preparation and characterization of human interleukin-5 expressed in recombinant Escherichia coli.

ABSTRACT: 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.

SUBMITTER: Proudfoot AE 

PROVIDER: S-EPMC1131729 | biostudies-other | 1990 Sep

REPOSITORIES: biostudies-other