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Study · Not a test of the peptide alone · 1992

5 results

[Synthesis of an artificial gene coding for thymosin alpha1 and its expression in Escherichia coli as a hybrid with human tumor necrosis factor].

Korobko VG, Boldyreva EF, Filippov SA, Berkova NP, Dobrynin VN, Shmelev VA, Popov SG, Evsegneev SI, Nosova LIu

Bioorganicheskaia khimiia1 May 1992Cited by 4 (Europe PMC)

PMID1417992 (opens in a new tab)PepBankPUB-01417992

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 study5

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

Studies that did not test the peptide alone5

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)Other

    An artificial gene encoding thymosin alpha‑1 was synthesised by a chemical-enzymatic method and cloned in Escherichia coli.

    In plain wordsIn bacteria, scientists made and cloned an artificial gene for thymosin alpha‑1.

    Outcome
    Not applicableSynthesis and cloning of an artificial thymosin alpha 1 gene
    Study

    Escherichia colin: not reported in source

    Escherichia coli
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    Chemical-enzymatic synthesis and cloning in Escherichia coli of an artificial gene encoding the immunoactive peptide thymosin alpha 1 have been carried out.

    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 aloneIn vitro (cells)Other

    In E. coli, the N-terminal TNF-thymosin alpha‑1 hybrid was secreted into the periplasmic space, while the C-terminal hybrid formed insoluble aggregates inside the cells.

    In plain wordsIn bacteria, one hybrid protein was secreted and the other clumped inside the cells.

    Outcome
    Not applicableLocation of hybrid proteins in E. coli
    Study

    Escherichia colin: not reported in source

    Escherichia coli
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    The N-terminal hybrid protein was secreted into periplasmic space, in contrast with the C-terminal hybrid protein, which formed insoluble aggregates inside bacterial cells.

    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.

  3. 03LabNot a test of Thymosin alpha-1 aloneIn vitro (cells)Activity measurement

    In mouse L-929 fibroblasts, the N-terminal hybrid protein showed full cytotoxic activity, while the C-terminal hybrid was much less active.

    In plain wordsIn lab tests on mouse cells, one hybrid protein was fully active and the other was much less active.

    Outcome
    Not applicableCytotoxic activity of hybrid proteins in L-929 cells
    Study

    mousen: not reported in source

    mouse fibroblast L-929
    Comparator
    C-terminal hybrid protein
    Outcome group
    Cell viability and death · Pharmacology

    Source sentences

    Summary
    The N-terminal hybrid protein displayed full biological activity in the cytotoxic assay on the mouse fibroblast L-929 whereas the C-terminal hybrid protein proved to be much less active.

    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.

  4. 04LabNot a test of Thymosin alpha-1 aloneIn vitro (cell-free)Other

    Isolation procedures were developed for both TNF-thymosin alpha‑1 hybrid proteins.

    In plain wordsIn lab work, scientists developed ways to purify both hybrid proteins.

    Outcome
    Not applicableIsolation procedures for hybrid proteins
    Study

    n: not reported in source

    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    Procedures for the isolation of both hybrid proteins were developed.

    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.

  5. 05LabNot a test of Thymosin alpha-1 aloneIn vitro (cell-free)Other

    Cyanogen bromide cleavage of TNF-thymosin alpha‑1 gave two polypeptides, and thymosin alpha‑1 was purified from them to homogeneity by simple chromatography.

    In plain wordsIn lab work, thymosin alpha‑1 was cut from the hybrid protein and purified by simple steps.

    Outcome
    Not applicableRelease and purification of thymosin alpha 1 from the hybrid protein
    Study

    n: not reported in source

    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    Treatment of the hybrid protein TNF-thymosin alpha 1 with cyanogen bromide lead to a mixture of two polypeptides, from which thymosin alpha 1 was purified to homogeneity by simple chromatographic procedures.

    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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