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Experientia1979; 35(3); 300-301; doi: 10.1007/BF01964311

Insensitivity of the ferritin iron core to heat treatment.

Abstract: To test whether the reactivity of ferritin iron is affected by the heat treatment used in ferritin isolation, we prepared ferritin from the same horse spleen with or without heating. Both samples exhibited similar reactivity upon reduction or chelation of iron.
Publication Date: 1979-03-15 PubMed ID: 446596DOI: 10.1007/BF01964311Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article is about the experiment conducted to determine the effect of heat treatment on ferritin iron reactivity sourced from horse spleen. The researchers found out that the reactivity of ferritin iron remains consistent whether it undergoes heat treatment during ferritin isolation or not.

Objective of the Study

  • The main goal of this research study is to determine the effect of heat treatment on the reactivity of ferritin iron. This is important in understanding how ferritin isolation processes might impact the outcomes of studies that utilize ferritin and ferritin iron.

Research Method

  • The researchers used ferritin from the same horse spleen as the subject of this study. The ferritin was prepared in two different ways – one subjected to heat treatment during ferritin isolation and the other not subjected to any heat treatment.
  • The reactivity of the ferritin in both samples was then tested. This was done by performing reduction or chelation of iron and observing the reactivity of the ferritin iron in each sample.

Findings of the Study

  • The results of the study showed that ferritin iron’s reactivity is not affected by heat treatment during ferritin isolation. Both the heat-treated sample and the non-heat-treated sample exhibited similar reactivity during the reduction or chelation of iron.
  • This suggests that the methods used in ferritin isolation, specifically heat treatment, do not have a significant impact on ferritin iron’s reactivity. Therefore, variations in ferritin isolation methods are unlikely to skew the results of studies that use ferritin and ferritin iron.

Importance and Implications of the Findings

  • The findings of this study are of significance to researchers in biological and medical fields. They provide valuable information about the stability of ferritin iron under varying thermal conditions which can influence experimental design and expected outcomes of studies involving ferritin and ferritin iron.
  • Since ferritin is often used in biomedical research, this finding confirms that regardless of the isolation method used, the reactivity of the ferritin iron remains constant, ensuring the reliability of experiment results.

Cite This Article

APA
Bertrand ML, Harris DC. (1979). Insensitivity of the ferritin iron core to heat treatment. Experientia, 35(3), 300-301. https://doi.org/10.1007/BF01964311

Publication

ISSN: 0014-4754
NlmUniqueID: 0376547
Country: Switzerland
Language: English
Volume: 35
Issue: 3
Pages: 300-301

Researcher Affiliations

Bertrand, M L
    Harris, D C

      MeSH Terms

      • Animals
      • Ferritins / isolation & purification
      • Ferritins / metabolism
      • Horses
      • Hot Temperature
      • Nitrilotriacetic Acid / pharmacology
      • Oxidation-Reduction
      • Spleen / analysis
      • Thioglycolates / pharmacology

      References

      This article includes 8 references
      1. Gonyea LM, Lamb CM, Sundberg RD, Deinard AS. Comparison of three procedures for isolating human ferritin, for use as a standard in an immunoradiometric assay.. Clin Chem 1976 Apr;22(4):513-8.
        pubmed: 1253434
      2. Harris DC. Iron exchange between ferritin and transferrin in vitro.. Biochemistry 1978 Jul 25;17(15):3071-8.
        pubmed: 698186doi: 10.1021/bi00608a020google scholar: lookup
      3. Niitsu Y, Listowsky I. Mechanisms for the formation of ferritin oligomers.. Biochemistry 1973 Nov 6;12(23):4690-5.
        pubmed: 4797990doi: 10.1021/bi00747a023google scholar: lookup
      4. Hoy TG, Harrison PM, Shabbir M. Uptake and release of ferritin iron. Surface effects and exchange within the crystalline core.. Biochem J 1974 Jun;139(3):603-7.
        pubmed: 4855331doi: 10.1042/bj1390603google scholar: lookup
      5. Brady GW, Kurkjian CR, Lyden EF, Robin MB, Saltman P, Spiro T, Terzis A. The structure of an iron core analog of ferritin.. Biochemistry 1968 Jun;7(6):2185-92.
        pubmed: 5660043doi: 10.1021/bi00846a022google scholar: lookup
      6. Pape L, Multani JS, Stitt C, Saltman P. The mobilization of iron from ferritin by chelating agents.. Biochemistry 1968 Feb;7(2):613-6.
        pubmed: 5644132doi: 10.1021/bi00842a015google scholar: lookup
      7. LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent.. J Biol Chem 1951 Nov;193(1):265-75.
        pubmed: 14907713
      8. Suran AA, Tarver H. Heterogeneity of horse spleen ferritin and apoferritin: comparison of electrophoretic and chromatographic fractions.. Arch Biochem Biophys 1965 Aug;111(2):399-406.
        pubmed: 5862001doi: 10.1016/0003-9861(65)90202-xgoogle scholar: lookup

      Citations

      This article has been cited 1 times.
      1. Kasztura M, Kiczak L, Pasławska U, Bania J, Janiszewski A, Tomaszek A, Zacharski M, Noszczyk-Nowak A, Pasławski R, Tabiś A, Kuropka P, Dzięgiel P, Ponikowski P. Hemosiderin Accumulation in Liver Decreases Iron Availability in Tachycardia-Induced Porcine Congestive Heart Failure Model. Int J Mol Sci 2022 Jan 18;23(3).
        doi: 10.3390/ijms23031026pubmed: 35162949google scholar: lookup