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Study · Not a test of the peptide alone · 1995

2 results

[Isolation of a group of hybrid proteins consisting of tumor necrosis factor alpha and thymosin alpha 1].

Shmelev VA, Bunina ZF, Kudriavtseva TIu, Zinchenko EV, Boldyreva EF, Korobko VG

Molekuliarnaia genetika, mikrobiologiia i virusologiia1 Jan 1995

PMID7603491 (opens in a new tab)PepBankPUB-07603491
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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 study2

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

Studies that did not test the peptide alone2

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. 01LabNot a test of Thymosin alpha-1 aloneIn vitro (cells)Activity measurement

    In L-929 cells, three TNF-thymosin alpha‑1 hybrid proteins differing in thymosin position showed different cytotoxicity.

    In plain wordsIn cells, hybrid proteins combining TNF and thymosin alpha‑1 differed in how toxic they were.

    Peptide
    Thymosin alpha-1
    Outcome
    MixedCytotoxicity of hybrid proteins in L-929 cells
    Study

    n: not reported in source

    L-929 cells
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    After dialysis the proteins displayed different cytotoxicity in L-929 cells and were fit for immunobiological studies.
    1 context sentence
    Summary · context
    New plasmid DNA coding for the synthesis of three hybrid proteins differing by the position of alpha 1-thymosin at N- and C-terminals of tumor necrosis factor were optimized and constructed.

    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.

  2. 02LabNot a test of Thymosin alpha-1 aloneOther designOther

    In E. coli expression, culturing temperature and protein structure affected the solubility of the TNF-thymosin alpha‑1 hybrid proteins.

    In plain wordsIn lab-grown bacteria, temperature and protein structure changed how well the hybrid proteins dissolved.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableHybrid protein solubility by culture temperature and structure
    Study

    n: not reported in source

    E. coli expression system
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    The effects of culturing temperature and protein structure on protein solubility were shown.

    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

    12 Oct 2026, 17:28 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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