Purification and biochemical characterization of human pluripotent hematopoietic colony-stimulating factor

Proc Natl Acad Sci U S A. 1985 Mar;82(5):1526-30. doi: 10.1073/pnas.82.5.1526.

Abstract

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 X 10(8) units/mg of protein.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Biological Assay
  • Cell Line
  • Colony-Stimulating Factors / isolation & purification*
  • Culture Media
  • Hematopoietic Stem Cells / physiology
  • Humans
  • Isoelectric Point
  • Molecular Weight
  • Urinary Bladder Neoplasms / analysis

Substances

  • Colony-Stimulating Factors
  • Culture Media