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. 1972 Feb;126(3):761–764. doi: 10.1042/bj1260761

The subunit structure of apoferritin and other eicosamers.

R R Crichton
PMCID: PMC1178438  PMID: 5075279

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Selected References

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

  1. Adams G. H., Schumaker V. N. Rapid molecular weight estimates for low-density lipoproteins. Anal Biochem. 1969 Apr 11;29(1):117–129. doi: 10.1016/0003-2697(69)90014-1. [DOI] [PubMed] [Google Scholar]
  2. Anderson P. J., Johnson P. A comparative study of the glutamate dehydrogenases isolated from bovine and chicken livers. Biochim Biophys Acta. 1969 May;181(1):45–51. doi: 10.1016/0005-2795(69)90225-6. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. Blombäck B., Blombäck M., Henschen A., Hessel B., Iwanaga S., Woods K. R. N-terminal disulphide knot of human fibrinogen. Nature. 1968 Apr 13;218(5137):130–134. doi: 10.1038/218130a0. [DOI] [PubMed] [Google Scholar]
  5. Blombäck B. The N-terminal disulphide knot of human fibrinogen. Br J Haematol. 1969 Aug;17(2):145–157. doi: 10.1111/j.1365-2141.1969.tb01353.x. [DOI] [PubMed] [Google Scholar]
  6. Bryce C. F., Crichton R. R. Gel filtration of proteins and peptides in the presence of 6M guanidine hydrochloride. J Chromatogr. 1971 Dec 23;63(2):267–280. doi: 10.1016/s0021-9673(01)85639-9. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Cornish-Bowden A. J., Koshland D. E., Jr The quaternary structure of proteins composed of identical subunits. J Biol Chem. 1971 May 25;246(10):3092–3102. [PubMed] [Google Scholar]
  9. Crichton R. R., Barbiroli V. Studies on the structure of horse spleen apoferritin. FEBS Lett. 1970 Jan 26;6(2):134–136. doi: 10.1016/0014-5793(70)80021-7. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. 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]
  12. Drysdale J. W. Microheterogeneity in ferritin molecules. Biochim Biophys Acta. 1970 Apr 28;207(1):256–258. doi: 10.1016/0005-2795(70)90158-3. [DOI] [PubMed] [Google Scholar]
  13. Easterbrook K. B. The arrangement of subunits in the shell of ferritin. Electron microscopic observations of molecules negatively stained with uranyl acetate. J Ultrastruct Res. 1970 Dec;33(5):442–450. doi: 10.1016/s0022-5320(70)90173-5. [DOI] [PubMed] [Google Scholar]
  14. Eisenberg H., Tomkins G. M. Molecular weight of the subunits, oligomeric and associated forms of bovine liver glutamate dehydrogenase. J Mol Biol. 1968 Jan 14;31(1):37–49. doi: 10.1016/0022-2836(68)90052-1. [DOI] [PubMed] [Google Scholar]
  15. FRIEDEN C. The molecular weight of chicken-liver glutamate dehydrogenase. Biochim Biophys Acta. 1962 Aug 13;62:421–423. doi: 10.1016/0006-3002(62)90274-3. [DOI] [PubMed] [Google Scholar]
  16. HARRISON P. M., HOFMANN T., MAINWARING W. I. The structure of apoferritin: amino acid composition and end-groups. J Mol Biol. 1962 Apr;4:251–256. doi: 10.1016/s0022-2836(62)80003-5. [DOI] [PubMed] [Google Scholar]
  17. HARRISON P. M., HOFMANN T., MAINWARING W. I. The structure of apoferritin: amino acid composition and end-groups. J Mol Biol. 1962 Apr;4:251–256. doi: 10.1016/s0022-2836(62)80003-5. [DOI] [PubMed] [Google Scholar]
  18. HARRISON P. M., HOFMANN T. The structure of apoferritin: evidence for chemical subunits from "fingerprints" of tryptic digests. J Mol Biol. 1962 Apr;4:239–250. doi: 10.1016/s0022-2836(62)80002-3. [DOI] [PubMed] [Google Scholar]
  19. Hanson K. R. Conformationally distinct subunits in protein oligomers with dihedral symmetry. J Mol Biol. 1968 Nov 28;38(1):133–136. doi: 10.1016/0022-2836(68)90134-4. [DOI] [PubMed] [Google Scholar]
  20. Hayakawa T., Kanzaki T., Kitamura T., Fukuyoshi Y., Sakurai Y., Koike K., Suematsu T., Koike M. Mammalian alpha-keto acid dehydrogenase complexes. V. Resolution and reconstitution studies of the pig heart pyruvate dehydrogenase complex. J Biol Chem. 1969 Jul 10;244(13):3660–3670. [PubMed] [Google Scholar]
  21. Hayes M. B., Wellner D. Microheterogeneity of L-amino acid oxidase. Separation of multiple components by polyacrylamide gel electrofucusing. J Biol Chem. 1969 Dec 25;244(24):6636–6644. [PubMed] [Google Scholar]
  22. Henney H. R., Jr, Willms C. R., Muramatsu T., Mukherjee B. B., Reed L. J. Alpha-keto acid dehydrogenase complexes. VII. Isolation and partial characterization of the polypeptide chains in the dihydrolipoyl transacetylase of Escherichia coli. J Biol Chem. 1967 Mar 10;242(5):898–901. [PubMed] [Google Scholar]
  23. Ishikawa E., Oliver R. M., Reed L. J. Alpha-Keto acid dehydrogenase complexes, V. Macromolecular organization of pyruvate and alpha-ketoglutarate dehydrogenase complexes isolated from beef kidney mitochondria. Proc Natl Acad Sci U S A. 1966 Aug;56(2):534–541. doi: 10.1073/pnas.56.2.534. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Lee J. C., Richter G. W. Ferritin from different organs of man, rat, rabbit and pig. Comp Biochem Physiol B. 1971 Jun 15;39(2):325–333. doi: 10.1016/0305-0491(71)90177-5. [DOI] [PubMed] [Google Scholar]
  25. Mainwaring W. I., Hofmann T. Horse spleen apoferritin: N-terminal and C-terminal residues. Arch Biochem Biophys. 1968 Jun;125(3):975–980. doi: 10.1016/0003-9861(68)90536-5. [DOI] [PubMed] [Google Scholar]
  26. McKee P. A., Rogers L. A., Marler E., Hill R. L. The subunit polypeptides of human fibrinogen. Arch Biochem Biophys. 1966 Sep 26;116(1):271–279. doi: 10.1016/0003-9861(66)90033-6. [DOI] [PubMed] [Google Scholar]
  27. Pollard H. B., Devi S. K. Construction of a three-dimensional iso-density map of the low-density lipoprotein particle from human serum. Biochem Biophys Res Commun. 1971 Aug 6;44(3):593–599. doi: 10.1016/s0006-291x(71)80124-9. [DOI] [PubMed] [Google Scholar]
  28. Pollard H., Scanu A. M., Taylor E. W. On the geometrical arrangement of the protein subunits of human serum low-density lipoprotein: evidence for a dodecahedral model. Proc Natl Acad Sci U S A. 1969 Sep;64(1):304–310. doi: 10.1073/pnas.64.1.304. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. 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]
  30. Urushizaki I., Niitsu Y., Ishitani K., Matsuda M., Fukuda M. Microheterogeneity of horse spleen ferritin and apoferritin. Biochim Biophys Acta. 1971 Aug 27;243(2):187–192. doi: 10.1016/0005-2795(71)90075-4. [DOI] [PubMed] [Google Scholar]
  31. Willms C. R., Oliver R. M., Henney H. R., Jr, Mukherjee B. B., Reed L. J. Alpha-keto acid dehydrogenase complexes. VI. Dissociation and reconstitution of the dihydrolipoyl transacetylase of Escherichia coli. J Biol Chem. 1967 Mar 10;242(5):889–897. [PubMed] [Google Scholar]

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