Nov 3, 1986

Purification and characterization of human interleukin-1 beta expressed in recombinant Escherichia coli

European Journal of Biochemistry
P WingfieldJ M Dayer

Abstract

The high-level expression of human interleukin-1 beta in Escherichia coli is described. The protein contributes about 12% of the total cell protein and is associated with the soluble cytoplasmic fraction of the cell. A method for the purification of the protein is given which is based on anion- and cation-exchange chromatographies. The isolated protein, shown to be homogeneous by several analytical methods, has been characterized by amino acid analysis, N- and C-terminal sequence analysis and analytical centrifugation. The protein is biologically active as demonstrated by two different in vitro assays, namely, the mononuclear cell factor (IL-1/MCF) assay and lymphocyte activating factor (IL-1/LAF) assay. The specific activities determined with the IL-1/MCF and IL-1/LAF assays, are 2 X 10(7) and 4 X 10(7) units mg-1, respectively.

Mentioned in this Paper

Shuttle Vectors
Mononuclear Cells
Alkalescens-Dispar Group
Carboxy-Terminal Amino Acid
Interleukin-1
Proteins, Recombinant DNA
Chromatography
Soluble
Sequence Analysis
Cations

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