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Purification and Characterization of an Immunoreactive Thymosin α1 from Human Blood

Evidence for a Thymosin α1 Carrier Protein
  • Jieping Chen
  • Teresa L. K. Low
  • Allan L. Goldstein
Part of the GWUMC Department of Biochemistry Annual Spring Symposia book series (GWUN)

Abstract

Thymosin α1 was first isolated from bovine thymus gland (Goldstein et al., 1977; Low et al., 1979). It is composed of 28 amino acid residues with a molecular weight of 3108 and an isoelectric point of 4.2. This peptide can stimulate lymphocytes to produce macrophage inhibitory factor (Thurman et al., 1981), interferon (Huang et al., 1981), and T-cell growth factor (Zatz et al., 1984). Thymosin α1 also modulates the expression of terminal deoxynucleotidyl transferase (TdT) in vivo and in vitro (Hu et al., 1981; Goldschneider et al., 1981).

Keywords

Terminal Deoxynucleotidyl Transferase Glycine Buffer Immunoaffinity Chromatography Thymic Hormone Chain Molecular Weight 
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.

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References

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Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Jieping Chen
    • 1
  • Teresa L. K. Low
    • 1
  • Allan L. Goldstein
    • 1
  1. 1.Department of BiochemistryThe George Washington University School of Medicine and Health SciencesUSA

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