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. 1986 May;5(5):871–876. doi: 10.1002/j.1460-2075.1986.tb04297.x

Purification and characterization of human granulocyte colony-stimulating factor (G-CSF).

H Nomura, I Imazeki, M Oheda, N Kubota, M Tamura, M Ono, Y Ueyama, S Asano
PMCID: PMC1166876  PMID: 3487449

Abstract

A colony-stimulating factor (CSF) has been purified to homogeneity from the serum-free medium conditioned by one of the human CSF-producing tumor cell lines, CHU-2. The molecule was a hydrophobic glycoprotein (mol. wt 19,000, pI = 6.1 as asialo form) with possible O-linked glycosides. Amino acid sequence determination of the molecule gave a single NH2-terminal sequence which had no homology to the corresponding sequence of the other CSFs previously reported. The biological activity was apparently specific for a neutrophilic granulocyte-lineage of both human and mouse bone marrow cells with a specific activity of 2.7 X 10(8) colonies/10(5) non-adherent human bone marrow cells/mg protein. The purified CSF can be regarded as a G-CSF of human origin and will become a useful material for investigation of regulatory mechanisms of human granulopoiesis.

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Selected References

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