Macrophage activation factor (MAF) was isolated from PPD-stimulated, BCG-immune mouse spleen cell culture fluids. In nine gel filtration runs on Sphadex G-100 or G-200, MAF was eluted in a single peak corresponding to a MW of 55,000 ± 1600. Recovery of activity was about 65%. Since the relative concentration curve of eluted MAF was wider than that of a single protein, MAF activity may be due to more than one protein with similar molecular weights. This possibility is strengthened by a broad elution range on DEAE cellulose chromatography, from a specific conductance of 3.5 to 8.5 mmho/cm, at pH 7.9 MAF was labile at both pH 4 and 10, and was destroyed by proteolytic enzymes. Eighty percent was destroyed by heating at 56°C for 30 min. In affinity chromatography experiments, MAF did not bind to Con-A Sepharose; but it was bound to insolubilized Cibacron-blue and was eluted by an increase in ionic strength.

Characterization of macrophage activation factor, a lymphokine that causes macrophages to become cytotoxic for tumor cells / Leonard, Ej; Ruco, Luigi; M. S., Meltzer. - In: CELLULAR IMMUNOLOGY. - ISSN 0008-8749. - 41:2(1978), pp. 347-357.

Characterization of macrophage activation factor, a lymphokine that causes macrophages to become cytotoxic for tumor cells

RUCO, Luigi;
1978

Abstract

Macrophage activation factor (MAF) was isolated from PPD-stimulated, BCG-immune mouse spleen cell culture fluids. In nine gel filtration runs on Sphadex G-100 or G-200, MAF was eluted in a single peak corresponding to a MW of 55,000 ± 1600. Recovery of activity was about 65%. Since the relative concentration curve of eluted MAF was wider than that of a single protein, MAF activity may be due to more than one protein with similar molecular weights. This possibility is strengthened by a broad elution range on DEAE cellulose chromatography, from a specific conductance of 3.5 to 8.5 mmho/cm, at pH 7.9 MAF was labile at both pH 4 and 10, and was destroyed by proteolytic enzymes. Eighty percent was destroyed by heating at 56°C for 30 min. In affinity chromatography experiments, MAF did not bind to Con-A Sepharose; but it was bound to insolubilized Cibacron-blue and was eluted by an increase in ionic strength.
1978
01 Pubblicazione su rivista::01a Articolo in rivista
Characterization of macrophage activation factor, a lymphokine that causes macrophages to become cytotoxic for tumor cells / Leonard, Ej; Ruco, Luigi; M. S., Meltzer. - In: CELLULAR IMMUNOLOGY. - ISSN 0008-8749. - 41:2(1978), pp. 347-357.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/458974
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