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    Home > Biochemistry News > Biotechnology News > Protein Carbonyl Determination Using Biotin Hydrazide

    Protein Carbonyl Determination Using Biotin Hydrazide

    • Last Update: 2020-12-20
    • Source: Internet
    • Author: User
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    Protein oxidation is a recognized component of aging and a consequence of severe or prolonged exposure to reactive oxygen species (ROS). Direct attack of protein by ROS causes formation of protein-bound carbonyl groups (
    1
    ). These carbonyl functions represent a variety of site-specific modifications, most particularly adipic and glutamic acid semialdehydes (
    2
    ). Additionally, numerous lipid oxidation products, including αβ-unsaturated γ-hydroxyalkenals can attack proteins yielding protein-bound aldehydes (
    3
    ). Furthermore, nonemzymatic glycation can yield protein-bound carbonyl functionalities (
    4
    ). Thus, protein carbonyls represent a possibly convenient indicator of oxidative stress. A variety of techniques have been introduced to measure protein carbonyls in tissue extracts, where they are found to increase exponentially as a function of organism aging (
    5
    ). All the extant techniques for protein carbonyl determination rely upon reductive amination between the carbonyl group and a probe, typically dinitrophenylhydrazine (DNPH) (
    5

    6
    ). Antibodies specific to the probe can then be used to visualize protein carbonyls.
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