Differences in subunit composition and iron content of isoferritins.
Abstract: Horse spleen ferritin was fractionated into its constituent isoferritins by isoelectric focusing. Separated isoferritins were stable and showed no tendency to redistribute when re-examined by analytical gel focusing. All of the isoferritins were immunologically indistinguishable when tested with antibodies raised against unfractionated horse spleen ferritin. The separated isoferritins also had similar conformations as determined by circular dichroism. Iron distribution studies, however, revealed a wide disparity among the isoferritins. The most acidic components had the lowest iron content but the iron content did not vary systematically throughout the isoferritin spectrum. Natural apoferritin, isolated from the ferritin by density gradient centrifugation, focused exclusively as the acidic moieties, whereas apoferritin prepared by reduction of native ferritin exhibited a banding pattern similar to that of unfractionated ferritin. The subunit structure of the isoferritins was examined by gel electrophoresis in sodium dodecyl sulfate or acidic urea systems. Multiple subunit types were demonstrated by both methods. The relative proportion of these subunit types varied progressively through the isoferritin spectrum. This difference in subunit population appears to be the basis for much of the structural heterogeneity in the apoferritin shells.
Publication Date: 1975-07-25 PubMed ID: 806592
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- Journal Article
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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The research investigates the variability in the composition and iron content in different variants of ferritin, a type of protein responsible for storing and releasing iron in the body. The study was performed on horse spleen ferritin and highlighted the disparities in iron content among different ferritin forms and the subunit structures that might contribute to these differences.
Research Methodology
- The research used horse spleen ferritin which was broken down into its constituent isoferritins or varying forms of ferritin through a process called isoelectric focusing.
- The researchers tested these separated isoferritins for stability and their tendency to disperse by re-analyzing them through gel focusing.
- Immunological tests with antibodies and circular dichroism were conducted to observe any structural differences among the separated isoferritins.
- To examine the distribution of iron among the different isoferritins, iron distribution studies were carried out.
- The researchers separated natural apoferritin, an iron-free form of ferritin, from ferritin through centrifugation and subjected it to focusing test to see its forms in terms of acidity.
- The research also studied the subunit structure of the isoferritins using gel electrophoresis in sodium dodecyl sulfate or acidic urea systems.
Research Findings
- The study found that all the isolated variants of ferritin were similar both immunologically and in their structural conformation as determined by circular dichroism, a technique used to study the structures of molecules.
- However, significant disparities were observed in the iron content across these variants. The most acidic components of the isoferritins were found to have the least amount of iron.
- Upon examining the natural apoferritin, it was determined that it focused exclusively as the acidic units. This suggests that these acidic units have least iron content, supporting the above finding.
- Gel electrophoresis revealed that multiple types of subunits were present in the isoferritins. Furthermore, the relative proportions of these subunit types varied through the isoferritin spectrum.
- The researchers concluded that this difference in subunit composition is key to the structural heterogeneity in the apoferritin shells, thus affecting the iron content of the isoferritins.
Conclusions and Implications
- The research provides important information on the variability in iron content across different isoferritins or ferritin variants.
- The insights from this study can help in understanding how variations in ferritin form may impact iron storage and release in the body, offering potential for targeted interventions in conditions related to iron imbalance.
Cite This Article
APA
Ishitani K, Listowsky I.
(1975).
Differences in subunit composition and iron content of isoferritins.
J Biol Chem, 250(14), 5446-5449.
Publication
Researcher Affiliations
MeSH Terms
- Animals
- Apoferritins / analysis
- Circular Dichroism
- Densitometry
- Ferritins / analysis
- Horses
- Immunodiffusion
- Iron / analysis
- Isoelectric Focusing
- Spleen
Citations
This article has been cited 5 times.- Masison J, Mendes P. Modeling the iron storage protein ferritin reveals how residual ferrihydrite iron determines initial ferritin iron sequestration kinetics.. PLoS One 2023;18(2):e0281401.
- Kim HJ, Kim HM, Kim JH, Ryu KS, Park SM, Jahng KY, Yang MS, Kim DH. Expression of heteropolymeric ferritin improves iron storage in Saccharomyces cerevisiae.. Appl Environ Microbiol 2003 Apr;69(4):1999-2005.
- Russell SM, Harrison PM. Heterogeneity in horse ferritins. A comparative study of surface charge, iron content and kinetics of iron uptake.. Biochem J 1978 Oct 1;175(1):91-104.
- Wagstaff M, Worwood M, Jacobs A. Properties of human tissue isoferritins.. Biochem J 1978 Sep 1;173(3):969-77.
- Hegenauer J, Saltman P, Hatlen L. Removal of cadmium(II) from crystallized ferritin.. Biochem J 1979 Feb 1;177(2):693-5.
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