Abstract
Interleukin-2 (IL-2) is a cytokine derived pendently to IL-2, but with more than from T-helper lymphocytes. Originally lOO-fold lower afflnity (I& = 10V9 M). known as T-cell growth factor it was Nevertheless, binding leads to internalidiscovered in the supernatants of PHAzation and activation. The o-chain, a 55 stimulated lymphocyte cultures.’ It is kDa protein, binds to IL-2 (& = 10e8) but produced constitutively by some T-cell does not lead to internalization. The leukaemias, and a gene from one of them appearance of the 55 kDa protein (CD 25) (Jurkat) has been transfected into Escheris a characteristic of cell activation, and ichia coli to produce large quantities of its function is to increase the affinity of the recombinant protein.2 the 75 kDa receptor. IL-2 has a single polypeptide chain of I33 amino acids which are internally linked by a single disulphide bond. The recombinant protein has a molecular weight of 15 kDa, but the naturallyoccurring cytokine is variably glycosylated. However, non-glycosylated recombinant protein appears identical to the natural product in its biological properties. MURINE EXPERIMENTS WITH IL-24
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