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Study · Not a test of the peptide alone · 2013

4 results

Thymosin β4 and tissue transglutaminase. Molecular characterization of cyclic thymosin β4.

App C, Knop J, Huff T, Sticht H, Hannappel E

The protein journal1 Aug 2013Cited by 2 (Europe PMC)

PMID23975143 (opens in a new tab)DOI10.1007/s10930-013-9507-0 (opens in a new tab)PepBankPUB-23975143
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

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone4

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. 01LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism

    Tβ4 served as a specific glutaminyl substrate for guinea pig transglutaminase.

    In plain wordsIn lab tests, an enzyme from guinea pig acted on Tβ4.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableTβ4 as substrate of guinea pig transglutaminase
    Study

    n: not reported in source

    purified Tβ4 and transglutaminase
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Thymosin β4 serves as a specific glutaminyl substrate for guinea pig transglutaminase.

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

    Without another aminyl donor, an ε-amino group of Tβ4 served as the aminyl substrate, an intramolecular bond formed and NH3 was lost, giving a product 16.3 Da lighter than Tβ4.

    In plain wordsIn lab tests, the enzyme made Tβ4 form a ring by itself, and the product was slightly lighter.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableFormation of cyclic Tβ4 with loss of NH3
    Study

    n: not reported in source

    purified Tβ4 and transglutaminase
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    In the absence of an appropriate additional aminyl donor an ε-amino group of thymosin β4 serves also as an aminyl substrate and an intramolecular bond is formed concomitantly NH3 (17 Da) is lost.
    2 context sentences
    Summary · context
    The molecular mass of the product is 4,949.6 Da.
    Summary · context
    This is 16.3 Da less than the molecular mass of thymosin β4 (4,965.9 Da).

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

    Only one isopeptide bond, between Lys16 and Gln36, formed in cyclic Tβ4 despite 3 glutaminyl and 9 lysyl residues.

    In plain wordsIn lab tests, only one ring-forming bond formed in Tβ4, at a specific pair of amino acids.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicablePosition of the isopeptide bond in cyclic Tβ4
    Study

    n: not reported in source

    purified Tβ4 and transglutaminase
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    In spite of 3 glutaminyl and 9 lysyl residues of thymosin β4 only one isopeptide bond between Lys16 and Gln36 was formed (cyclic thymosin β4).

    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).

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

    Cyclic Tβ4 still formed a complex with G-actin, but the complex was about one fiftieth as stable as the Tβ4-G-actin complex.

    In plain wordsIn lab tests, ring-shaped Tβ4 still bound actin, but much more weakly than normal Tβ4.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    DecreaseComplex stability of cyclic Tβ4 with G-actin
    Study

    n: not reported in source

    purified Tβ4 and transglutaminase
    Comparator
    Linear Tβ4
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Cyclic thymosin β4 still forms a complex with G-actin albeit the stability of the complex is about one fiftieth of the stability of the thymosin β4 × G-actin complex.

    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.

Publication types

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