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)


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).


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