Biological Activity of Recombinant Human Interleukin-2 Produced in <i>Escherichia coli</i>

TLDR

The IL‑2 gene from Jurkat cells and normal lymphocytes was cloned into *E. coli*, yielding high‑yield recombinant protein that was purified to homogeneity and assayed in vitro and in vivo.

Abstract

The gene for interleukin-2 was isolated from the Jurkat cell line and from normal peripheral blood lymphocytes and, when inserted in Escherichia coli, was expressed at high concentrations. This interleukin-2 was purified to apparent homogeneity and tested for biological activity in a variety of assays in vitro and in vivo. The recombinant lymphokine supports the growth of murine and human interleukin-2 dependent cell lines, enhances the generation of murine and human cytolytic cells in vitro, and generates lymphokine activated killer cells from murine and human lymphocytes. It has a serum half-life of 2 to 3 minutes in the mouse and significantly enhances the generation of cytolytic cells in vivo after alloimmunization. No functional differences between native and the recombinant interleukin-2 molecules have been detected.