The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Purification and biochemical characterization of human pluripotent hematopoietic colony-stimulating factor.
Open accessAbstract
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.
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Cites
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Metadata
- Authors
- Welte, K., Platzer, E., Lu, L., Gabrilove, J. L., Levi, E., Mertelsmann, R., & Moore, M. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1985-03
- Volume
- 82
- Issue
- 5
- Pages
- 1526-1530
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2068021117
- Cited by
- 517
- References
- 15
- FWCI
- 23.24
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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