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 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.
Monti
E
E
Department of Biomedical Sciences and Biotechnology, University of Brescia, Italy.
Pozzi
A
A
Tiberio
L
L
Morelli
D
D
Caruso
A
A
Villa
M L
ML
Balsari
A
A
D015153:Blotting, Western; D002846:Chromatography, Affinity; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology / Q000302:isolation & purification*; D007376:Interleukin-2 / Q000276:immunology / Q000302:isolation & purification*; D008213:Lymphocyte Activation / Q000276:immunology; D008214:Lymphocytes / Q000276:immunology; D011863:Radioimmunoassay; D011994:Recombinant Proteins; D012685:Sepharose
D007074:Immunoglobulin G; D007376:Interleukin-2; D011994:Recombinant Proteins; D012685:Sepharose