Characterization of Immunoaffinity-Purified Human T-Cell Growth Factor from JURKAT Cells

  • Terry D. Copeland
  • Kendall A. Smith
  • Stephen Oroszlan
Part of the GWUMC Department of Biochemistry Annual Spring Symposia book series (GWUN)


T-cell growth factor (TCGF) is a lymphokine that was first identified in conditioned media of mitogen-activated human T-cell culture (Morgan et al., 1976). TCGF also occurs in other mammalian systems and its biological properties were recently reviewed (Smith, 1983). TCGF proved to be essential for the isolation of human T-cell leukemia virus. For a recent review see Gallo and Wong-Staal (1982).


JURKAT Cell Bovine Leukemia Virus Intact Protein Acetonitrile Concentration Nucleic Acid Binding Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Clark, S. C., Arya, S. K., Wong-Staal, F., Matsumoto-Kobayashi, M., Kay, R. M., Kaufman, R. J., Brown, E. L., Shoemaker, C., Copeland, T., Oroszlan, S., Smith, K., Sarngadharan, M. G., Lindner, S. G., and Gallo, R. C., 1984, Human T-cell growth factor: Partial amino acid sequence, cDNA cloning, and organization and expression in normal and leukemic cells, Proc. Natl. Acad. Sci. USA (in press).Google Scholar
  2. Copeland, T. D., Grandgenett, D. P., and Oroszlan, S., 1980, Amino acid sequence analysis of reverse transcriptase subunits from avian myeloblastosis virus, J. Virol. 36:115–119.PubMedGoogle Scholar
  3. Copeland, T. D., Morgan, M. A., and Oroszlan, S., 1983, Complete amino acid sequence of the nucleic acid binding protein of bovine leukemia virus, FEBS Lett. 156:37–40.PubMedCrossRefGoogle Scholar
  4. Edman, P., and Begg, G., 1967, A protein sequenator, Eur. J. Biochem. 1:80–91.PubMedCrossRefGoogle Scholar
  5. Gallo, R. C., and Wong-Staal, F., 1982, Retroviruses as etiologic agents of some animal and human leukemias and lymphomas and as tools for elucidating the molecular mechanism of leukemogenesis, Blood 60:545–557.PubMedGoogle Scholar
  6. Henderson, L. E., Copeland, T. D., Sowder, R. C., Smythers, G. W., and Oroszlan, S., 1981, Primary structure of the low-molecular-weight nucleic acid binding proteins of murine leukemia viruses, J. Biol Chem. 256:8400–8406.PubMedGoogle Scholar
  7. Hopp, T. P., and Woods, K. R., 1981, Prediction of protein antigenic determinants from amino acid sequences, Proc. Natl. Acad. Sci. USA 78:3824–3828.PubMedCrossRefGoogle Scholar
  8. Mier, J. W., and Gallo, R. C., 1980, Purification and some characteristics of human T-cell growth factor from phytohemagglutinin-stimulated lymphocyte-conditioned media, Proc. Natl. Acad. Sci. 77:6134–6138.PubMedCrossRefGoogle Scholar
  9. Morgan, D. A., Ruscetti, F. W., and Gallo, R. C., 1976, Selective in vitro growth of T lymphocytes from normal human bone marrows, Science 193:1007–1008.PubMedCrossRefGoogle Scholar
  10. Oroszlan, S., Henderson, L. E., Stephenson, J. R., Copeland, T. D., Long, C. W., Ihle, J. N., and Gilden, R. V., 1978, Amino- and carboxyl-terminal amino acid sequences of proteins coded by gag gene of murine leukemia virus, Proc. Natl. Acad. Sci. USA 75:1404–1408.PubMedCrossRefGoogle Scholar
  11. Robb, R. J., and Smith, K. A., 1981, Heterogeneity of human T-cell growth factor (TCGF) due to variable glycosylation, Mol. Immunol. 18:1087–1094.PubMedCrossRefGoogle Scholar
  12. Smith, K. A., 1983, T-cell growth factor, a lymphocytotrophic hormone, in: Genetics of the Immune Response (G. Moller, ed.), pp. 151–185, Plenum Press, New York.CrossRefGoogle Scholar
  13. Smith, K. A., Favata, M. F., and Oroszlan, S., 1983, Production and characterization of monoclonal antibodies to human interleukin-2, J. Immunol. 131:1808–1815.PubMedGoogle Scholar
  14. Taniguchi, T., Matsui, H., Fujita, T., Takaoka, C., Kashima, N., Yoshimoto, R., and Hamuro, J., 1983, Structure and expression of a cloned cDNA for human interleukin-2, Nature (London) 302:305–310.CrossRefGoogle Scholar
  15. Tarr, G. E., Beecher, J. F., Bell, M., and McKean, D. J., 1978. Polyquatemary amines prevent peptide loss from sequenators, Anal. Biochem. 84:622–627.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Terry D. Copeland
    • 1
  • Kendall A. Smith
    • 2
  • Stephen Oroszlan
    • 1
  1. 1.Laboratory of Molecular Virology and Carcinogenesis, LBI-Basic Research ProgramNCI-Frederick Cancer Research FacilityFrederickUSA
  2. 2.Department of MedicineDartmouth Medical SchoolHanoverUSA

Personalised recommendations