PURIFICATION OF INTERLEUKIN-2 ANTIBODIES FROM HEALTHY-INDIVIDUALS

By covalent binding of recombinant interleukin-2 (rIL-2) to Sepharose, it was possible to immunopurify specific human anti-IL-2 antibodies f rom a pool of immunoglobulins obtained from healthy subjects. Since lo w quantities of the ligand released by the matrix could interfere with the evaluation of the biological activity of anti-IL-2 antibodies, th e antibody preparation was subjected to pepsin digestion which is know n to destroy the IL-2 molecule. Purified human anti-IL-2 antibodies we re found to be mostly IgG1 and able to neutralize IL-2 induced periphe ral blood lymphocytes (PBL) proliferation in vitro. The availability o f purified anti-IL-2 antibodies, obtained from healthy individuals, ab le to modulate IL-2 activity, could be important in several therapeuti c approaches.