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Purification and Biochemical Characterization of Human Pluripotent Hematopoietic Colony-Stimulating Factor
Karl Welte, Erich Platzer, Li Lu, Janice L. Gabrilove, Ester Levi, Roland Mertelsmann and Malcolm A. S. Moore
Proceedings of the National Academy of Sciences of the United States of America
Vol. 82, No. 5 (Mar. 1, 1985), pp. 1526-1530
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/25444
Page Count: 5
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Pluripotent hematopoietic colony-stimulating factor (pluripotent CSF), a protein that is constitutively produced by the human bladder carcinoma cell line 5637, has been purified from low serum (0.2% fetal calf serum)-containing conditioned medium. The purification involved sequential ammonium sulfate precipitation, ion-exchange chromatography, gel filtration, and reversed-phase high-performance liquid chromatography. The purified protein has a molecular weight of 18,000 in NaDodSO4/polyacrylamide gel electrophoresis, both by the silver staining technique and by elution of biological activity from a corresponding gel slice, and has an isoelectric point of 5.5. Pluripotent CSF supports the growth of human mixed colonies, granulocyte-macrophage colonies, and early erythroid colonies and induces differentiation of the human promyelocytic leukemic cell line HL-60 and the murine myelomonocytic leukemic cell line WEHI-3B (D+). The specific activity of the purified pluripotent CSF in the granulocyte-macrophage colony assay is 1.5× 108 units/mg of protein.
Proceedings of the National Academy of Sciences of the United States of America © 1985 National Academy of Sciences