| Literature DB >> 2205201 |
A E Proudfoot1, D Fattah, E H Kawashima, A Bernard, P T Wingfield.
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.Entities:
Mesh:
Substances:
Year: 1990 PMID: 2205201 PMCID: PMC1131729 DOI: 10.1042/bj2700357
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857