Purification of interleukin-2 antibodies from healthy individuals

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

doi:10.1016/0165-2478(93)90098-M

Purification of interleukin-2 antibodies from healthy individuals

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

Fondazione IRCCS Istituto Nazionale dei Tumori

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	261-266
Number of pages	6
Journal	Immunology Letters
Volume	36
Issue number	3
DOIs	https://doi.org/10.1016/0165-2478(93)90098-M
Publication status	Published - 1993

Keywords

Affinity chromatography
Interleukin 2
Natural antibody

ASJC Scopus subject areas

Immunology
Immunology and Allergy

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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.",

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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

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JO - Immunology Letters

JF - Immunology Letters

SN - 0165-2478

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Purification of interleukin-2 antibodies from healthy individuals

Abstract

Keywords

ASJC Scopus subject areas

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