PMID: 6969402Oct 1, 1980Paper

Purification and some characteristics of human T-cell growth factor from phytohemagglutinin-stimulated lymphocyte-conditioned media

Proceedings of the National Academy of Sciences of the United States of America
J W Mier, R C Gallo

Abstract

Human T-cell growth factor (TCGF), a mitogenic protein that appears in the media of cultured lymphocytes after phytohemagglutinin-stimulation, has been purified more than 400-fold from serum-free conditioned media by using a sequence of ion exchange chromatography and gel filtration. The purified growth factor elutes as a broad peak from DEAE-Sepharose, focuses diffusely at a pH of about 6.8 on isoelectric focusing (suggesting heterogeneity in electrical charge), has an estimated molecular weight of approximately 23,000 as judged by gel filtration (12,000-13,000 on Na-DodSO4/polyacrylamide gel electrophoresis), is resistant to DNase and RNase, is degraded by trypsin, and does not adhere to any of several lectin-Sepharoses. These characteristics indicate that it is nonglycosylated and protein in nature. The activity of the factor determined by cell counts or [3H]thymidine incorporation in human T lymphoblasts, is stable at room temperature in crude conditioned media, but the partially purified factor requires the addition of albumin or polyethylene glycol to maintain stability. Unlike the crude conditioned media, the purified factor lacks colony-stimulating activity and, unlike lectins, antigens, and crude conditioned media, it ...Continue Reading

References

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Citations

May 1, 1990·Journal of Neuroscience Research·G M Jonakait, S Schotland
Jan 1, 1981·Journal of Cancer Research and Clinical Oncology·J MinowadaT Ohnuma
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