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. 1973 Apr;131(4):855–857. doi: 10.1042/bj1310855

The subunit structure of horse spleen apoferritin: the molecular weight of the oligomer and its stability to dissociation by dilution (Short Communication)

Robert R Crichton 1,*, Robert Eason 1, Allan Barclay 1, Charles F A Bryce 1
PMCID: PMC1177546  PMID: 4737327

Abstract

The oligomer molecular weight of horse spleen apoferritin was determined by sedimentation-equilibrium techniques and a value of 443000 found. It is concluded that the apoferritin molecule consists of 24 subunits. At concentrations as low as 0.01μm there is no evidence of subunit dissociation.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bjork I., Fish W. W. Native and subunit molecular weights of apoferritin. Biochemistry. 1971 Jul 20;10(15):2844–2848. doi: 10.1021/bi00791a007. [DOI] [PubMed] [Google Scholar]
  2. Bryce C. F., Crichton R. R. The subunit structure of horse spleen apoferritin. I. The molecular weight of the subunit. J Biol Chem. 1971 Jul 10;246(13):4198–4205. [PubMed] [Google Scholar]
  3. Crichton R. R., Bryce C. F.A. Molecular weight estimation of apoferritin sub-units. FEBS Lett. 1970 Jan 26;6(2):121–124. doi: 10.1016/0014-5793(70)80017-5. [DOI] [PubMed] [Google Scholar]
  4. Crichton R. R. Ferritin: structure, synthesis and function. N Engl J Med. 1971 Jun 24;284(25):1413–1422. doi: 10.1056/NEJM197106242842506. [DOI] [PubMed] [Google Scholar]
  5. Crichton R. R., Millar J. A., Cumming R. L., Bryce C. F. The organ-specificity of ferritin in human and horse liver and spleen. Biochem J. 1973 Jan;131(1):51–59. doi: 10.1042/bj1310051. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Crichton R. R. Studies on the structure of ferritin and apoferritin from horse spleen. I. Tryptic digestion of ferritin and apoferritin. Biochim Biophys Acta. 1969 Nov 11;194(1):34–42. doi: 10.1016/0005-2795(69)90176-7. [DOI] [PubMed] [Google Scholar]
  7. Crichton R. R. The subunit structure of apoferritin and other eicosamers. Biochem J. 1972 Feb;126(3):761–764. doi: 10.1042/bj1260761. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. HARRISON P. M. The structure of apoferritin: molecular size, shape and symmetry from x-ray data. J Mol Biol. 1963 May;6:404–422. doi: 10.1016/s0022-2836(63)80052-2. [DOI] [PubMed] [Google Scholar]
  9. Jaenicke R., Bartmann P. Dissociation-association properties of apoferritin in the milligram and microgram range. Biochem Biophys Res Commun. 1972 Nov 15;49(4):884–890. doi: 10.1016/0006-291x(72)90295-1. [DOI] [PubMed] [Google Scholar]
  10. Pape L., Multani J. S., Stitt C., Saltman P. In vitro reconstitution of ferritin. Biochemistry. 1968 Feb;7(2):606–612. doi: 10.1021/bi00842a014. [DOI] [PubMed] [Google Scholar]
  11. Rice R. H., Means G. E. Radioactive labeling of proteins in vitro. J Biol Chem. 1971 Feb 10;246(3):831–832. [PubMed] [Google Scholar]
  12. Richter G. W., Walker G. F. Reversible association of apoferritin molecules. Comparison of light-scattering and other data. Biochemistry. 1967 Sep;6(9):2871–2880. doi: 10.1021/bi00861a031. [DOI] [PubMed] [Google Scholar]
  13. YPHANTIS D. A. EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS. Biochemistry. 1964 Mar;3:297–317. doi: 10.1021/bi00891a003. [DOI] [PubMed] [Google Scholar]

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