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The Biochemical journal1973; 131(1); 51-59; doi: 10.1042/bj1310051

The organ-specificity of ferritin in human and horse liver and spleen.

Abstract: 1. Ferritin was isolated from human and horse spleen and liver, and apoferritin prepared therefrom. 2. The electrophoretic mobilities of the four apoferritins were determined on polyacrylamide gels and on cellulose acetate strips, and all found to be equal. 3. Homologous ferritins share reactions of identity in immunodiffusion experiments, whereas heterologous ferritins show only partial identity. 4. The subunit molecular weight of each of the apoferritins was determined by polyacrylamide-gel electrophoresis in sodium dodecyl sulphate and by chromatography on agarose columns in 6m-guanidine-HCl. A value of approx. 18500 was found in all cases. The proteins all had sedimentation coefficients of 17-18S. It thus seems that they have identical quaternary structures. 5. The amino acid compositions of the proteins revealed distinct differences both between organs and between species. This was confirmed by analysis of the tryptic peptide patterns, where it was found that about one-third of the peptides were common to the four proteins and the other two-thirds varied from protein to protein. 6. It is concluded that the apoferritins present in the liver and spleen of human and horse are both organ- and species-specific. 7. The apoferritin isolated from the liver of a patient with idiopathic haemochromatosis was identical with normal human liver apoferritin by the criteria described above.
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Publication Date: 1973-01-01 PubMed ID: 4198584PubMed Central: PMC1177438DOI: 10.1042/bj1310051Google Scholar: Lookup
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  • Journal Article

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.

This research paper investigates the ferritin (a type of protein that stores iron) in human and horse liver and spleen. The study concludes that these ferritins may have identical structures, but show distinct differences in their amino acid composition depending on both the type of organ and the species.

Research Methodology

  • The researchers extracted ferritin from the spleens and livers of human and horses. They then prepared these extracted ferritins into a form called apoferritin.
  • The mobility (movement under influence of electric field) of each of these four different apoferritins was analyzed using two different techniques, one involving polyacrylamide gels and the other using cellulose acetate strips. In both methods, the mobility was found to be identical.

Experimental Observations

  • The investigators carried out immunodiffusion experiments, where they observed that ferritins from the same species had identical reactions while those from different species (human and horse) showed only partial similarity.
  • The subunit molecular weight of each apoferritin was determined by electrophoresis in sodium dodecyl sulphate and by chromatography on agarose columns. All apoferritins had a molecular weight of approximately 18500 and had similar sedimentation coefficients, indicating identical quaternary structures.

Amino Acid Compositions

  • The researchers followed up by investigating the amino acid compositions of these apoferritins. Results indicated distinct differences between ferritins extracted from different organs and those from different species.
  • This grouping was also confirmed when analyzing the patterns of tryptic peptides, with about one-third of these peptides shared among the four apoferritins, and the other two-thirds varied based on the specific protein sample.

Conclusion

  • From the data, it was concluded that despite the identical structure, the apoferritins present in the liver and spleen of human and horses are both organ- and species-specific.
  • The apoferritin isolated from the liver of a patient with idiopathic haemochromatosis (a condition causing one to absorb too much iron from their diet) was identical to that of a normal human liver based on the criteria applied in this research.

Cite This Article

APA
Crichton RR, Millar JA, Cumming RL, Bryce CF. (1973). The organ-specificity of ferritin in human and horse liver and spleen. Biochem J, 131(1), 51-59. https://doi.org/10.1042/bj1310051

Publication

The Biochemical journal
ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 131
Issue: 1
Pages: 51-59

Researcher Affiliations

Crichton, R R
    Millar, J A
      Cumming, R L
        Bryce, C F

          MeSH Terms

          • Aged
          • Amino Acid Sequence
          • Amino Acids / analysis
          • Animals
          • Apoproteins / analysis
          • Centrifugation, Density Gradient
          • Chromatography
          • Chromatography, Gel
          • Electrophoresis, Polyacrylamide Gel
          • Ferritins / analysis
          • Ferritins / isolation & purification
          • Guanidines
          • Hemochromatosis / metabolism
          • Horses
          • Humans
          • Immunodiffusion
          • Liver / analysis
          • Male
          • Molecular Weight
          • Organ Specificity
          • Peptides / analysis
          • Rabbits / immunology
          • Species Specificity
          • Spleen / analysis
          • Ultrafiltration

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