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. 1981 Jul 1;197(1):171–175. doi: 10.1042/bj1970171

The composition and the structure of bacterioferritin of Escherichia coli.

J Yariv, A J Kalb, R Sperling, E R Bauminger, S G Cohen, S Ofer
PMCID: PMC1163067  PMID: 7032515

Abstract

Bacterioferritin isolated from Escherichia coli is of two kinds: a protein containing a polynuclear iron compound, the bacterioferritin proper and a protein free of the polynuclear iron compound, the apo-bacterioferritin. Bacterioferritin of both kinds is characterized by absorption maxima at 417,530 and 560 nm, contributed by protohaem IX. Single crystals of bacterioferritin of the space group I432 suggest that the molecule is made up of 24 identical subunits related by a cubic point symmetry. The molecular weight of the protein subunit, as determined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, is 15000. In the electron microscope the bacterioferritin molecule appears to be a sphere of 9.5 nm (95 A) diameter composed of a negatively staining outer shell and an inner electron-dense core of 6 nm (60 A) diameter.

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Selected References

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

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