Purification and characterization of human interleukin-1beta expressed in recombinant Escherichia coli Academic Article uri icon

  •  
  • Overview
  •  
  • Research
  •  
  • Identity
  •  
  • Additional Document Info
  •  
  • View All
  •  

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.

authors

  • WINGFIELD, Paul
  • PAYTON, Mark
  • TAVERNIER, Jean
  • BARNES, Marjory
  • SHAW, Alan
  • ROSE, Keith
  • SIMONA, Marco G
  • Demczuk, Suzanne
  • WILLIAMSON, Karen
  • DAYER, Jean-Michel

publication date

  • November 1986

has subject area