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[Antioxidant properties of proteins after freezing-thawing].

Abstract: Experimental data are presented which were obtained under comparative evaluation of influence of different freezing-thawing conditions on antioxidant properties of isolated proteins: human serum albumin, cytochrome c from the horse heart and glucose oxidase from Aspergillus niger. The observed protein antioxidant activity alterations are assumed to be a result of protein conformational changes. The character of freezing-thawing influence on the protein antioxidant activity depends on the molecular structure and cooling conditions.
Publication Date: 2012-06-12 PubMed ID: 22679758
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  • Journal Article

Summary

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The research article discusses an experiment that evaluated how different freezing-thawing conditions affect the antioxidant properties of certain isolated proteins – human serum albumin, cytochrome c from the horse heart and glucose oxidase from Aspergillus niger. The article suggests that changes in protein antioxidant activity observed are due to protein conformational changes and that the effect of freezing-thawing on the protein antioxidant activity depends on the molecular structure and cooling conditions.

Explanation of the Research

  • The study presents data from experiments that were conducted to assess the impact of various freezing-thawing conditions on the antioxidant characteristics of specially isolated proteins.
  • The proteins studied include human serum albumin (a protein in human blood), cytochrome c from the heart of a horse (a component that plays a key role in the energy production of cells), and glucose oxidase from Aspergillus niger (an enzyme from a type of fungus that is able to break down glucose).

Key Observations and Assumptions

  • The researchers observed changes in the antioxidant activity of these proteins after the freezing-thawing process. Antioxidants are substances that inhibit oxidation in the cells of the body, preventing damage from free radicals.
  • These changes in antioxidant activity are believed to be due to conformational changes in the proteins. Conformational changes refer to the alteration in the shape or structure of a protein molecule. These changes can affect a protein’s functionality, including its antioxidant activity.

Impact of Molecular Structure and Cooling Conditions

  • Notably, the study found that the effect of the freezing-thawing process on protein antioxidant activity was dependent on both the molecular structure of the protein and the cooling conditions.
  • This means that the way a protein is structured at a molecular level, as well as the specific conditions under which it is frozen and thawed, can significantly influence its antioxidant properties.

Cite This Article

APA
Rozanova SL, Rozanova ED, Nardid OA. (2012). [Antioxidant properties of proteins after freezing-thawing]. Ukr Biokhim Zh (1999), 84(1), 53-59.

Publication

NlmUniqueID: 101657175
Country: Ukraine
Language: rus
Volume: 84
Issue: 1
Pages: 53-59

Researcher Affiliations

Rozanova, S L
    Rozanova, E D
      Nardid, O A

        MeSH Terms

        • Animals
        • Antioxidants / chemistry
        • Aspergillus niger
        • Benzothiazoles / chemistry
        • Cryopreservation
        • Cytochromes c / chemistry
        • Ferrous Compounds / chemistry
        • Ferrozine / chemistry
        • Freezing
        • Glucose Oxidase / chemistry
        • Horses
        • Humans
        • Protein Conformation
        • Serum Albumin / chemistry
        • Solutions
        • Spectrophotometry
        • Sulfonic Acids / chemistry

        Citations

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