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.
Original language | English |
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Pages (from-to) | 261-266 |
Number of pages | 6 |
Journal | Immunology Letters |
Volume | 36 |
Issue number | 3 |
DOIs | |
Publication status | Published - 1993 |
Keywords
- Affinity chromatography
- Interleukin 2
- Natural antibody
ASJC Scopus subject areas
- Immunology
- Immunology and Allergy