Skip to content

Study · In vitro (cell-free) · 1994

6 results

The sulfoxide of thymosin beta 4 almost lacks the polymerization-inhibiting capacity for actin.

Heintz D, Reichert A, Mihelic-Rapp M, Stoeva S, Voelter W, Faulstich H

European journal of biochemistry1 Jul 1994Cited by 15 (Europe PMC)

PMID8055902 (opens in a new tab)DOI10.1111/j.1432-1033.1994.tb19000.x (opens in a new tab)PepBankPUB-08055902
Publisher pagePubMedAsk about this study
Jump to 6 results

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 study6

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

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

    In a cell-free system, an equimolar amount of thymosin beta‑4 almost completely prevented actin polymerization, whereas the same amount of its sulfoxide allowed polymerization similar to pure actin.

    In plain wordsIn lab tests, an equal amount of thymosin beta‑4 almost completely stopped actin from forming filaments, but its oxidized form did not.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    DecreaseInhibition of actin polymerization by thymosin beta 4
    Study

    n: not reported in source

    Comparator
    Thymosin beta 4 sulfoxide
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    While an equimolar amount of T beta 4 prevented actin polymerization almost completely
    1 context sentence
    Title · context
    The sulfoxide of thymosin beta 4 almost lacks the polymerization-inhibiting capacity for actin.
  2. 02LabIn vitro (cell-free)Activity measurement

    In a cell-free system, under non-polymerizing conditions thymosin beta‑4 bound actin with an affinity of approximately 1 microM, equal to that of its sulfoxide.

    In plain wordsIn lab tests, thymosin beta‑4 bound actin with an affinity of about 1 microM, the same as its oxidized form.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableThymosin beta 4 affinity for actin under non-polymerizing conditions
    Study

    n: not reported in source

    Comparator
    Thymosin beta 4 sulfoxide
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    Affinity for actin
    ≈ 1 µM
    non-polymerizing conditions

    Source sentences

    Summary
    Interestingly, under non-polymerizing conditions, the affinity of T beta 4 sulfoxide for actin is as high as that of T beta 4 (approximately 1 microM).
  3. 03LabIn vitro (cell-free)Activity measurement

    In cross-linking experiments with actin monomer, thymosin beta‑4 gave a 47-kDa actin-conjugate band, in amounts similar to its sulfoxide.

    In plain wordsIn lab tests, thymosin beta‑4 formed a complex with actin monomer in amounts similar to its oxidized form.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableActin monomer cross-linking by thymosin beta 4
    Study

    n: not reported in source

    Comparator
    Thymosin beta 4 sulfoxide
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    In accordance with this, no differences were found between T beta 4 and the sulfoxide in cross-linking experiments with the monomer, where both forms of the peptide yielded similar amounts of a 47-kDa band representing conjugates of actin and beta-thymosin, as proved by Western-blotting analysis.
  4. 04LabIn vitro (cell-free)Activity measurement

    In a cell-free system, thymosin beta‑4 retarded the exchange of G-actin-bound nucleotide, to a similar extent as its sulfoxide.

    In plain wordsIn lab tests, thymosin beta‑4 slowed nucleotide exchange on actin, to the same extent as its oxidized form.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    DecreaseG-actin-bound nucleotide exchange with thymosin beta 4
    Study

    n: not reported in source

    Comparator
    Thymosin beta 4 sulfoxide
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Likewise, both, T beta 4 and the sulfoxide retarded the exchange of G-actin-bound nucleotide to similar extents.

Studies that did not test the peptide alone2

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. 05LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Activity measurement

    In a cell-free system, the methionine sulfoxide derivative of thymosin beta‑4 inhibited actin polymerization about 20 times less than thymosin beta‑4.

    In plain wordsIn lab tests, the oxidized form of thymosin beta‑4 blocked actin filament formation about 20 times less than thymosin beta‑4.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    DecreaseInhibition of actin polymerization by thymosin beta 4 sulfoxide
    Study

    n: not reported in source

    Comparator
    Thymosin beta 4
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Measurements

    Relative inhibition vs thymosin beta 4
    ≈ 20 times less
    actin polymerization

    Source sentences

    Summary
    T beta 4 sulfoxide inhibits actin polymerization to an extent approximately 20-times less than T 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).

  2. 06LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Activity measurement

    In a cell-free system, the sulfoxide derivative of thymosin beta‑4 had a 20-times lower affinity to actin than thymosin beta‑4.

    In plain wordsIn lab tests, the oxidized form of thymosin beta‑4 bound actin about 20 times less tightly than thymosin beta‑4.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    DecreaseActin affinity of thymosin beta 4 sulfoxide under polymerizing conditions
    Study

    n: not reported in source

    Comparator
    Thymosin beta 4
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Measurements

    Relative affinity to actin
    ≈ 20 times lower
    sulfoxide vs thymosin beta 4

    Source sentences

    Summary
    We showed that the decrease in the inhibitory activity is reflected by a 20-times lower affinity to 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).

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.

PepBank is a research reference. Talk to a doctor before you use any peptide.