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Study · In vitro (cell-free) · 1996

4 results

The ternary complex of DNase I, actin and thymosin beta4.

Reichert A, Heintz D, Echner H, Voelter W, Faulstich H

FEBS letters1 Jun 1996Cited by 9 (Europe PMC)

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

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

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

    Cross-linking of thymosin beta4 to the actin-DNase I complex occurred to the same extent as with pure actin, at a somewhat lower rate.

    In plain wordsIn lab tests, thymosin beta4 linked to actin that already held DNase I as much as to actin alone, but a bit slower.

    Outcome
    Not applicableCross-linking of Tbeta4 to the actin-DNase I complex
    Study

    n: not reported in source

    purified proteins
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    In the present study this method was used to show that such crosslinking, which is indicative of complex formation, occurs to the same extent with the actin-DNase I complex as with pure actin, although at a somewhat lower rate.
  2. 02LabIn vitro (cell-free)Activity measurement

    Gel electrophoresis gave further evidence for formation of a ternary complex of DNase I, actin and thymosin beta4.

    In plain wordsIn lab tests, a gel test also showed that DNase I, actin and thymosin beta4 can form one complex.

    Outcome
    Not applicableGel electrophoresis evidence of the ternary complex
    Study

    n: not reported in source

    purified proteins
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Further evidence for the formation of the ternary complex was given by gel electrophoresis.
    1 context sentence
    Summary · context
    In the present study this method was used to show that such crosslinking, which is indicative of complex formation, occurs to the same extent with the actin-DNase I complex as with pure actin, although at a somewhat lower rate.
  3. 03LabIn vitro (cell-free)Activity measurement

    The KD value of thymosin beta4 from the actin-DNase I complex was identical to that from pure actin.

    In plain wordsIn lab tests, thymosin beta4 bound actin with DNase I just as tightly as it bound actin alone.

    Outcome
    No significant changeKD of Tbeta4 for the actin-DNase I complex
    Study

    n: not reported in source

    purified proteins
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    From fluorescence spectroscopy the KD value of Tbeta4 from the actin-DNase I complex was found to be identical to that from pure actin.
    1 context sentence
    Summary · context
    In the present study this method was used to show that such crosslinking, which is indicative of complex formation, occurs to the same extent with the actin-DNase I complex as with pure actin, although at a somewhat lower rate.
  4. 04LabIn vitro (cell-free)Activity measurement

    The capacity of actin for inhibiting DNase I was not affected by the addition of thymosin beta4.

    In plain wordsIn lab tests, adding thymosin beta4 did not change how well actin blocked DNase I.

    Outcome
    No significant changeInhibition of DNase I by actin with Tbeta4
    Study

    n: not reported in source

    purified proteins
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    In line with these data, the capacity of actin for inhibiting DNase I was not affected by the addition of Tbeta4.
    1 context sentence
    Summary · context
    In the present study this method was used to show that such crosslinking, which is indicative of complex formation, occurs to the same extent with the actin-DNase I complex as with pure actin, although at a somewhat lower rate.

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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