Purification of interleukin-2 antibodies from healthy individuals

Eugenio Monti, Ambra Pozzi, Laura Tiberio, Daniele Morelli, Arnaldo Caruso, Maria Luisa Villa, Andrea Balsari

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)261-266
Number of pages6
JournalImmunology Letters
Volume36
Issue number3
DOIs
Publication statusPublished - 1993

Keywords

  • Affinity chromatography
  • Interleukin 2
  • Natural antibody

ASJC Scopus subject areas

  • Immunology
  • Immunology and Allergy

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