The release of iron from horse spleen ferritin to 1,10-phenanthroline.
Abstract: The rate of release of iron to 1,10-phenanthroline from ferritin fractions of different iron contents has been studied. The experimental results could be interpreted by a simple hypothetical model of the shape of the hydrous ferric oxide micelle at different iron contents, and reasonable correlation obtained between the rate of release and the calculated micelle surface areas. Initial rates of release did not correlate significantly with protein concentration.
Publication Date: 1974-01-01 PubMed ID: 4856608PubMed Central: PMC1166081DOI: 10.1042/bj1370067Google Scholar: Lookup
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- Journal Article
Summary
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The research investigates how iron is released from horse spleen ferritin to 1,10-phenanthroline and how this process relates to the structure of the hydrous ferric oxide micelle, which holds the iron inside the ferritin.
Introduction
- This study examines the process by which iron is released from a protein complex known as ferritin, present in horse spleen, to 1,10-phenanthroline, an organic compound often used in chemistry to test for the presence of metal ions.
Ferritin and Iron Release
- Ferritin is a protein complex that stores iron in a soluble and non-toxic form. When needed, the iron can be released from ferritin for use in various biological processes.
- The scientists observed this iron release process, but they didn’t only record the rate of the release. They also investigated the relationship between the rate and the specific condition of the ferritin fractions, namely their iron content.
Hypothetical Model for Iron Release
- Analysis of experimental results led to the creation of a simple hypothetical model relating to the form of hydrous ferric oxide micelle at different iron contents.
- A micelle, in this case, refers to a form in which hydrous ferric oxide (an iron compound that includes water in its structure) is arranged within the ferritin. This arrangement or ‘shape’ can influence the iron release rate.
- The model showed a significant correlation between the rate of iron release and calculated micelle surface areas. This means that the release rate was not random, but related to the micelle’s characteristics, such as its surface area.
Role of Protein Concentration
- Interestingly, while the model illustrated the relationship between iron release rate and micelle surface area, there seemed to be no significant correlation between the initial rates of release and the concentration of the protein.
- This implies that the iron release process might be influenced more by the state of the micelle within the ferritin, rather than the amount of protein present in the solution.
Cite This Article
APA
Hoy TG, Harrison PM, Shabbir M, Macara IG.
(1974).
The release of iron from horse spleen ferritin to 1,10-phenanthroline.
Biochem J, 137(1), 67-70.
https://doi.org/10.1042/bj1370067 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Centrifugation, Density Gradient
- Colloids
- Ferritins
- Horses
- Iron
- Kinetics
- Macromolecular Substances
- Mathematics
- Models, Biological
- Phenanthrolines
- Spectrophotometry
- Spleen
- Time Factors
References
This article includes 8 references
- Fischbach FA, Anderegg JW. An x-ray scattering study of ferritin and apoferritin.. J Mol Biol 1965 Dec;14(2):458-73.
- Haggis GH. The iron oxide core of the ferritin molecule.. J Mol Biol 1965 Dec;14(2):598-602.
- Jones MM, Johnston DO. Rate of release of iron from ferritin to 1, 10-phenanthroline.. Nature 1967 Nov 4;216(5114):509-10.
- Harrison PM, Fischbach FA, Hoy TG, Haggis GH. Ferric oxyhydroxide core of ferritin.. Nature 1967 Dec 23;216(5121):1188-90.
- Macara IG, Hoy TG, Harrison PM. The formation of ferritin from apoferritin. Kinetics and mechanism of iron uptake.. Biochem J 1972 Jan;126(1):151-62.
- Macara IG, Hoy TG, Harrison PM. The formation of ferritin from apoferritin. Catalytic action of apoferritin.. Biochem J 1973 Oct;135(2):343-8.
- LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent.. J Biol Chem 1951 Nov;193(1):265-75.
- FARRANT JL. An electron microscopic study of ferritin.. Biochim Biophys Acta 1954 Apr;13(4):569-76.
Citations
This article has been cited 10 times.- Huang HQ, Lin QM, Kong B, Zeng RY, Qiao YH, Chen CH, Zhang FZ, Xu LS. Role of phosphate and kinetic characteristics of complete iron release from native pig spleen ferritin-Fe.. J Protein Chem 1999 May;18(4):497-504.
- Treffry A, Harrison PM. Non-random distribution of iron entering rat liver ferritin in vivo.. Biochem J 1984 Jun 15;220(3):857-9.
- Hoy TG, Harrison PM, Shabbir M. Uptake and release of ferritin iron. Surface effects and exchange within the crystalline core.. Biochem J 1974 Jun;139(3):603-7.
- Harrison PM, Hoy TG, Macara IG, Hoare RJ. Ferritin iron uptake and release. Structure-function relationships.. Biochem J 1974 Nov;143(2):445-51.
- Sirivech S, Frieden E, Osaki S. The release of iron from horse spleen ferritin by reduced flavins.. Biochem J 1974 Nov;143(2):311-5.
- O'Connell MJ, Ward RJ, Baum H, Peters TJ. The role of iron in ferritin- and haemosiderin-mediated lipid peroxidation in liposomes.. Biochem J 1985 Jul 1;229(1):135-9.
- O'Connell MJ, Ward RJ, Baum H, Peters TJ. Iron release from haemosiderin and ferritin by therapeutic and physiological chelators.. Biochem J 1989 Jun 15;260(3):903-7.
- Joo MS, Tourillon G, Sayers DE, Theil EC. Rapid reduction of iron in horse spleen ferritin by thioglycolic acid measured by dispersive X-ray absorption spectroscopy.. Biol Met 1990;3(3-4):171-5.
- Trefry A, Harrison PM. Incorporation and release of inorganic phosphate in horse spleen ferritin.. Biochem J 1978 May 1;171(2):313-20.
- Treffry A, Harrison PM. The binding of ferric iron by ferritin.. Biochem J 1979 Sep 1;181(3):709-16.
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