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 |
|---|---|
| Pages (from-to) | 261-266 |
| Number of pages | 6 |
| Journal | Immunology Letters |
| Volume | 36 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1993 |
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Keywords
- Affinity chromatography
- Interleukin 2
- Natural antibody
ASJC Scopus subject areas
- Immunology
- Immunology and Allergy
Cite this
Purification of interleukin-2 antibodies from healthy individuals. / Monti, Eugenio; Pozzi, Ambra; Tiberio, Laura; Morelli, Daniele; Caruso, Arnaldo; Villa, Maria Luisa; Balsari, Andrea.
In: Immunology Letters, Vol. 36, No. 3, 1993, p. 261-266.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification of interleukin-2 antibodies from healthy individuals
AU - Monti, Eugenio
AU - Pozzi, Ambra
AU - Tiberio, Laura
AU - Morelli, Daniele
AU - Caruso, Arnaldo
AU - Villa, Maria Luisa
AU - Balsari, Andrea
PY - 1993
Y1 - 1993
N2 - 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.
AB - 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.
KW - Affinity chromatography
KW - Interleukin 2
KW - Natural antibody
UR - http://www.scopus.com/inward/record.url?scp=0027312818&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027312818&partnerID=8YFLogxK
U2 - 10.1016/0165-2478(93)90098-M
DO - 10.1016/0165-2478(93)90098-M
M3 - Article
VL - 36
SP - 261
EP - 266
JO - Immunology Letters
JF - Immunology Letters
SN - 0165-2478
IS - 3
ER -