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Study · In vitro (cell-free) · 2003

1 result

DETECTION AND REMOVAL OF LEAD USING LEAD-BINDING PROTEINS

LOWE Adrian M., COLPAS Gerard J., HAMILTON Maureen A, SALCIUS Michael J., SANDERS Mitchell C.

Journal not recorded11 Dec 2002

PepBankPUB-95628950
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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 study1

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

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

    In a patent abstract, thymosin beta‑4 and the other listed proteins were described as binding lead in cell-free binding, with a high-affinity region of dissociation constant about 10-9 M; the abstract does not say which protein this value belongs to.

    In plain wordsIn lab tests, thymosin beta‑4 and other listed proteins were described as binding lead tightly.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableLead binding affinity
    Study

    n: not reported in source

    Lead-binding proteins
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Thymosin beta-4 (TB4), Thymosin beta-9 (TB9), and acyl-CoA binding protein (ACBP) are two proteins that possess the ability to bind lead in human tissue. These two proteins have a high affinity lead-binding region with a dissociation constant (Kd) of about 10-9 M that allows for a strong interaction…

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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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