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Study · Other design · 1979

2 results

The chemistry and biology of thymosin. I. Isolation, characterization, and biological activities of thymosin alpha1 and polypeptide beta1 from calf thymus.

Low TL, Thurman GB, McAdoo M, McClure J, Rossio JL, Naylor PH, Goldstein AL

The Journal of biological chemistry1 Feb 1979Cited by 185 (Europe PMC)

Summary

A partially purified extract from thymus tissue termed thymosin Fraction 5 has been shown to reconstitute immunological deficiencies resulting from the lack of thymic function in several animal models, as well as humans with primary and secondary immunodeficiency diseases. Thymosin Fraction 5 consists of a family of polypeptides with molecular weights ranging from 1,000 to 15,000. Several of these polypeptides contribute individually to the biological activity of the parent compound. Two polypeptide components of thymosin Fraction 5, termed thymosin alpha1 and polypeptide beta1, have been characterized chemically and biologically. Thymosin alpha1 is a highly acidic molecule composed of 28 amino acid residues. This polypeptide has potent biological activity and has been found to be 10 to 1,000 times as active as thymosin Fraction 5 in one in vivo and several in vitro bioassay systems designed to measure differentiation and function of thymus-dependent lymphocytes (T cells). Polypeptide beta1, in contrast, is inactive in our bioassay systems, suggesting that it is not involved in thymic hormone action. Sequence analysis and homology studies have indicated that polypeptide beta1, although present in Fraction 5, does not contribute to the biological activity of thymosin Fraction 5.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study2

1 result from studies that gave the peptide. No result from this study comes from people.

  1. 01LabOther designActivity measurement

    Thymosin alpha1 was 10 to 1,000 times as active as thymosin Fraction 5 in one in vivo and several in vitro bioassays of T-cell differentiation and function.

    In plain wordsIn one in vivo and several lab bioassays, thymosin alpha1 was much more active than the partly purified thymosin Fraction 5 extract.

    Outcome
    IncreaseActivity relative to thymosin Fraction 5 in T-cell bioassays
    Study

    n: not reported in source

    Thymosin alpha1 from calf thymus
    Comparator
    Thymosin Fraction 5
    Outcome group
    Immune response · Immune and inflammation
    Studied dose
    Dose not stated

    Source sentences

    Summary
    This polypeptide has potent biological activity and has been found to be 10 to 1,000 times as active as thymosin Fraction 5 in one in vivo and several in vitro bioassay systems designed to measure differentiation and function of thymus-dependent lymphocytes (T cells).

Studies that did not test the peptide alone1

In this study, Thymosin alpha-1 was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking Thymosin alpha-1.

  1. 02LabNot a test of Thymosin alpha-1 aloneIn vitro (cell-free)Other

    Thymosin alpha1 is a highly acidic molecule composed of 28 amino acid residues.

    In plain wordsIn lab tests, thymosin alpha1 was found to be a highly acidic molecule of 28 amino acids.

    Outcome
    Not applicableSize of thymosin alpha1
    Study

    n: not reported in source

    Thymosin alpha1 from calf thymus
    Outcome group
    Peptide structure and chemistry · Pharmacology

    Measurements

    Amino acid residues
    28 residues
    thymosin alpha1

    Source sentences

    Summary
    Thymosin alpha1 is a highly acidic molecule composed of 28 amino acid residues.

    In this study, Thymosin alpha-1 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin alpha-1.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 3Current

    10 Oct 2026, 08:55 UTC

    Study results updated

  2. Version 2

    9 Oct 2026, 03:03 UTC

    Study data updated · source update from Europe PMC

  3. Version 1

    9 Oct 2026, 03:02 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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