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Study · In vitro (cell-free) · 1993

4 results

Actin-sequestering ability of thymosin beta 4, thymosin beta 4 fragments, and thymosin beta 4-like peptides as assessed by the DNase I inhibition assay.

Hannappel E, Wartenberg F

Biological chemistry Hoppe-Seyler1 Feb 1993Cited by 33 (Europe PMC)

PMID8471179 (opens in a new tab)DOI10.1515/bchm3.1993.374.1-6.117 (opens in a new tab)PepBankPUB-08471179
Publisher pagePubMedAsk about this study
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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study4

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

  1. 01LabIn vitro (cell-free)Activity measurement

    In a DNase I inhibition assay, thymosin beta‑4 sequestered G-actin at a 1 to 1 ratio and inhibited its polymerisation to F-actin in high salt solution.

    In plain wordsIn lab tests, thymosin beta‑4 bound actin one to one and stopped it from forming filaments.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    DecreaseG-actin sequestration and inhibition of polymerization
    Study

    n: not reported in source

    DNase I inhibition assay with G-actin
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Thymosin beta 4 sequesters G-actin at a 1 to 1 ratio an thereby inhibits its polymerisation to F-actin in high salt solution.

Studies that did not test the peptide alone3

In this study, Thymosin beta-4 (human) 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 beta-4 (human).

  1. 02LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Activity measurement

    In a DNase I inhibition assay, oxidation of the single methionine at position 6 of thymosin beta‑4 did not abolish its actin-sequestering properties.

    In plain wordsIn lab tests, oxidized thymosin beta‑4 still bound actin like the unmodified peptide.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    No significant changeActin sequestration by oxidized thymosin beta 4 (methionine 6)
    Study

    n: not reported in source

    DNase I inhibition assay with G-actin
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    The oxidation of the single methionine residue at position 6 does not abolish its actin-sequestering properties.

    In this study, Thymosin beta-4 (human) 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 beta-4 (human).

  2. 03LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Activity measurement

    In a DNase I inhibition assay, neither thymosin beta‑4 fragment 24-43 nor fragment 13-43 inhibited the polymerisation of G-actin.

    In plain wordsIn lab tests, two shortened fragments of thymosin beta‑4 did not stop actin from forming filaments.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    No significant changePolymerisation of G-actin with thymosin beta 4 fragments 24-43 and 13-43
    Study

    n: not reported in source

    DNase I inhibition assay with G-actin
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    However neither thymosin beta 4 24-43 nor thymosin beta 4 13-43 inhibit the polymerisation of G-actin.

    In this study, Thymosin beta-4 (human) 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 beta-4 (human).

  3. 04LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Activity measurement

    In a DNase I inhibition assay, oxidized thymosin beta‑4 (beta 4-sulfoxide) and four other thymosin beta‑4-like peptides were actin-sequestering peptides like thymosin beta‑4.

    In plain wordsIn lab tests, oxidized thymosin beta‑4 and four related peptides bound actin like thymosin beta‑4.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    IncreaseActin sequestration by oxidized thymosin beta 4 and four thymosin beta 4-like peptides
    Study

    n: not reported in source

    DNase I inhibition assay with G-actin
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Oxidized thymosin beta 4 (beta 4-sulfoxide) as well as four other thymosin beta 4-like peptides were shown to be actin-sequestering peptides like thymosin beta 4.

    In this study, Thymosin beta-4 (human) 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 beta-4 (human).

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 2Current

    13 Oct 2026, 01:52 UTC

    Study results updated

  2. Version 1

    12 Oct 2026, 18:17 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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