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  • Title: Purification of the T lymphocyte growth factor interleukin-2 from culture media of human peripheral blood leukocytes (buffy coats).
    Author: Kniep EM, Kniep B, Grote W, Conradt HS, Monner DA, Mühlradt PF.
    Journal: Eur J Biochem; 1984 Aug 15; 143(1):199-203. PubMed ID: 6332022.
    Abstract:
    Interleukin 2 was purified 100 000-fold to apparent homogeneity from the supernatants of mitogen-stimulated human blood leukocytes. A sequence of three purification steps was used: affinity chromatography on the bound dye cibacron blue, gel filtration on Ultrogel AcA44, and reversed-phase high-performance liquid chromatography on hexyl phase. The resulting interleukin 2 had a specific activity of 2 X 10(6) U/mg protein, and was free of pyrogenicity in the rabbit test. The final purification product showed two bands in sodium dodecyl sulfate/polyacrylamide gels with apparent molecular masses of 15 kDa and 17 kDa respectively. Both bands were biologically active.
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