| Literature DB >> 8370597 |
E Monti1, A Pozzi, L Tiberio, D Morelli, A Caruso, M L Villa, A Balsari.
Abstract
By covalent binding of recombinant interleukin-2 (rIL-2) to Sepharose, it was possible to immunopurify specific human anti-IL-2 antibodies from a pool of immunoglobulins obtained from healthy subjects. Since low quantities of the ligand released by the matrix could interfere with the evaluation of the biological activity of anti-IL-2 antibodies, the antibody preparation was subjected to pepsin digestion which is known to destroy the IL-2 molecule. Purified human anti-IL-2 antibodies were found to be mostly IgG1 and able to neutralize IL-2 induced peripheral blood lymphocytes (PBL) proliferation in vitro. The availability of purified anti-IL-2 antibodies, obtained from healthy individuals, able to modulate IL-2 activity, could be important in several therapeutic approaches.Entities:
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Year: 1993 PMID： 8370597 DOI： 10.1016/0165-2478(93)90098-m
Source DB: PubMed Journal: Immunol Lett ISSN： 0165-2478 Impact factor: 3.685