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- W2427125280 abstract "The production of human interleukin-la (IL-la) in Escherichia coli is described together with a method for its purification. The isolated protein was shown to be pure and physically homogeneous. The in vitro biological activity of IL-1 a was tested with the mononuclear-cell factor and the lymphocyte-activating factor assays. The specific activity determined with both assays was about 3 x lo7 units mg-' and is similar to that observed with recombinant human IL-1 j. The purified protein was resolved by chromatofocusing into two species of isoelectric points 5.45 and 5.20 (75% and 25%, respectively, of the total protein). Both species had similar chemical properties and biological activities to the unfractionated protein. The charge difference between the species was attributed to the deamidation of a single Asn or Gln residue. The term interleukin-1 (IL-1) describes at least two monocyte-derived polypeptide hormones termed IL-1 a and IL-lB. These lymphokines appear responsible for a wide range of physiological responses to infection and injury including immune stimulation, inflammation, the acute-phase response and fever (for reviews see [l, 21). Recently the coding sequences for the IL-1 proteins have been cloned [3, 41. Using published sequence data we have isolated a cDNA for IL-la and have produced this protein in Escherichiu coli. In this report we describe the purification, some physicochemical properties and the biological activity of the recombinant DNA product." @default.
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- W2427125280 date "1987-01-01" @default.
- W2427125280 modified "2023-09-24" @default.
- W2427125280 title "Purification and characterization of human interleukin-la produced in Escherichia coli" @default.
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