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J. Biochem, 1988, Vol. 103, No. 4 661-666
© 1988 Japanese Biochemical Society

research-article

Characterization and Partial Purification of a Non-Interferon Macrophage Activating Factor Produced by Human Leukemic T Cell Line

Hiroshi Kutsukake*, Katsuyuki Imai*, Takayuki Harada**, Shigeru Morikawa** and Atsushi Tanaka*

*Departments of Biochemistry, Shimane Medical University Izumo, Shimane 693
**Departments of Pathology, Shimane Medical University Izumo, Shimane 693

Culture supernatants from several human leukemic T cell lines were found to contain a macrophage activating factor which enhanced hydrogen peroxide release from human peripheral blood monocyte-derived macrophages. The macrophage activating factor from a T cell line, CCRF-CEM, was characterized biochemically and compared with interferon-{gamma}, which is also an immunological product of T cells and has a potent macrophage activating activity. In contrast to interferon-{gamma}, the macrophage activating factor in the culture supernatants bound to an anion exchanger and did not adsorb onto concanavalin A gel. Culture supernatants and active fractions from chromatographies were essentially devoid of anti-viral activity. Anti-human interferon-{gamma} monoclonal antibody also failed to neutralize the macrophage activating factor from CCRF-CEM. MAF was eluted in the fractions with molecular weight of 40,000 to 60,000 on gel filtration in the presence of a detergent and a salt. MAF was partially purified to about 1,300-fold by the methods described above: chromatography with anion exchangers and gel filtration. It was concluded that MAF from CCRF-CEM was biochemically and immunologically different from interferon-{gamma}.


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