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The Biochemical journal1968; 110(2); 265-280; doi: 10.1042/bj1100265

Electron-microscopic and chemical studies of oligomers in horse ferritin.

Abstract: Horse ferritin was fractionated both by starch-gel electrophoresis and by gel filtration on Sephadex G-200. Monomer fractions contained up to 98% of monomer and oligomer fractions up to 76% of oligomers as determined by quantitative electron microscopy. Percentages obtained from electron micrographs correlated well with analytical starch-gel electrophoretograms and ultracentrifuge patterns. Amino acid analyses of monomer- and oligomer-enriched fractions showed no significant differences. Ferritin oligomers did not apparently dissociate on dilution for electron microscopy or on storage. Apoferritin dimers were stable in 0.01m-phosphate buffer at dilutions down to 0.19mg./ml. as shown by ultracentrifugation. Chemical studies indicated that the intermolecular bonds in oligomers are resistant to a variety of reagents and conditions, including those that would be expected to attack disulphide, peptide and ester linkages respectively. Partial disaggregation was achieved at high pH values and in 67% (v/v) acetic acid. Centre-to-centre intermolecular distances in dimers were found to be about 100å. Three main types of trimer configuration were found and a variety of tetramers and pentamers. These configurations are described and discussed.
Publication Date: 1968-11-01 PubMed ID: 5726206PubMed Central: PMC1187206DOI: 10.1042/bj1100265Google Scholar: Lookup
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  • Journal Article

Summary

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This research paper investigates the structure and chemical properties of oligomers present in horse ferritin, using techniques such as electron microscopy and gel filtration. Researchers also studied the stability and resistance of these oligomers under various conditions and treatments.

Section 1: Fractionation and analysis of ferritin

  • The study begins with the fractionation of horse ferritin by starch-gel electrophoresis and gel filtration on Sephadex G-200.
  • The monomer fractions contained up to 98% of monomer while oligomer fractions included up to 76% of oligomers.
  • The researchers relied on quantitative electron microscopy to determine these percentages and found that the results correlated well with analytical starch-gel electrophoretograms and ultracentrifuge patterns.

Section 2: Examining Amino Acids and Oligomers Stability

  • Amino acid analyses of both monomer and oligomer-enriched fractions showed no significant differences, which suggests that they are structurally similar.
  • Ferritin oligomers, clusters of ferritin molecules, did not dissociate upon dilution for electron microscopy or storage, indicating their stability.
  • Apoferritin dimers, pairs of apoferritin which are protein shells of ferritin without iron, were found to be stable in 0.01m-phosphate buffer at dilutions down to 0.19mg./ml as evidenced by ultracentrifugation.

Section 3: Examination of Intermolecular Bonds in Oligomers

  • The study involved chemical analysis to identify and understand the intermolecular bonds in oligomers.
  • The bonds were found to be resistant to a variety of reagents and conditions, which would typically attack disulphide, peptide, and ester linkages.
  • However, partial disaggregation of the bonds was achieved at high pH values and in a 67% acetic acid solution.

Section 4: Specific Configurations of Ferritin Oligomers

  • The centre-to-centre intermolecular distances in dimers were found to be about 100ångström, which is a unit of length equal to one hundred millionth of a centimetre.
  • The researchers found three main types of trimer, a molecule made up of three monomers, configurations, and various types of tetramers, a four-part molecule, and pentamers, a five-part molecule.
  • The study provides descriptions and discussions about these different molecular configurations, which could help in understanding their structures and characteristics better.

Cite This Article

APA
Williams MA, Harrison PM. (1968). Electron-microscopic and chemical studies of oligomers in horse ferritin. Biochem J, 110(2), 265-280. https://doi.org/10.1042/bj1100265

Publication

ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 110
Issue: 2
Pages: 265-280

Researcher Affiliations

Williams, M A
    Harrison, P M

      MeSH Terms

      • Animals
      • Chromatography, Gel
      • Electrophoresis
      • Ferritins / analysis
      • Horses
      • Hydrogen-Ion Concentration
      • Microscopy, Electron
      • Polymers / analysis
      • Ultracentrifugation

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