Isolation, purification and characterization of spleen ferritin of Gallus domesticus L.

Benito, F.F. Santos; Mateo, MaC. Martin

doi:10.1016/0305-0491(83)90243-2

Cited by 8 publications

(3 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We therefore examined whether the CE ferritoid-ferritin complexes also have these properties. For these analyses, to decrease the possibility of the results being affected by irrelevant proteins, we used lysates enriched for ferritin proteins by heat treatment 27,32 (described in Materials and Methods). For CE cells, this procedure generated lysates that consisted of two major bands by SDS-PAGE, one of 19 kDa and another of 30 kDa.…”

Section: Resultsmentioning

confidence: 99%

Nuclear Ferritin: A Ferritoid-Ferritin Complex in Corneal Epithelial Cells

Nurminskaya

Talbot

Nurminsky

et al. 2009

Invest. Ophthalmol. Vis. Sci.

View full text Add to dashboard Cite

Purpose Ferritin is an iron storage protein that is generally cytoplasmic. However, in embryonic avian corneal epithelial (CE) cells, the authors previously observed that the ferritin was predominantly nuclear. They also obtained evidence that this ferritin protects DNA from oxidative damage by UV light and hydrogen peroxide and that the nuclear localization involves a tissue-specific nuclear transporter, termed ferritoid. In the present investigation, the authors have determined additional properties of the nuclear ferritoid-ferritin complexes. Methods For biochemical characterization, a combination of molecular sieve chromatography, immunoblotting, and nuclear-cytoplasmic fractionation was used; DNA binding was analyzed by electrophoretic mobility shift assay. Results The CE nuclear ferritin complex has characteristics that differentiate it from a “typical” cytoplasmic ferritin, including the presence of ferritin and ferritoid subunits; a molecular weight of approximately 260 kDa, which is approximately half that of cytoplasmic ferritin; its iron content, which is below our limits of detection; and its ability to bind to DNA. Conclusions Within CE cell nuclei, ferritin and ferritoid are coassembled into stable complex(es) present in embryonic and adult corneas. Thus, ferritoid not only serves transiently as a nuclear transporter for ferritin, it remains as a component of a unique ferritoid-ferritin nuclear complex.

show abstract

Section: Resultsmentioning

confidence: 99%

Nuclear Ferritin: A Ferritoid-Ferritin Complex in Corneal Epithelial Cells

Nurminskaya

Talbot

Nurminsky

et al. 2009

Invest. Ophthalmol. Vis. Sci.

View full text Add to dashboard Cite

show abstract

“…Researchers have made notable improvements in ferritin purification methods. For example, Worwood et al replaced the previous combination of heating and ion exchange chromatography with immunoadsorption and ion exchange chromatography, resulting in better purification of serum ferritin; 58 Pagéet al successfully purified normal human liver ferritin using a highly reproducible method based on the unique thermal stability and molecular weight of ferritin, involving ultrafiltration, S-300 gel filtration, and DEAE-Affi Gel Blue purification; 59 Santos Benito and Martin Mateo simplified the separation and purification steps, obtaining chicken spleen ferritin with electrophoretic purity through only two steps of salting out and Sephadex G-200 chromatography; 60 Cham et al used the methanol−heat treatment method to rapidly separate human liver ferritin while maintaining its antigenicity. 61 In addition, since the successful isolation and purification of pea ferritin in 1962, several plant ferritins have been purified and developed.…”

Section: Preparation and Identification Of Ferritinmentioning

confidence: 99%

Advancements of the Molecular Directed Design and Structure–Activity Relationship of Ferritin Nanocage

Xia,

Li,

Zang

et al. 2024

J. Agric. Food Chem.

View full text Add to dashboard Cite

Ferritin nanocages possess remarkable structural properties and biological functions, making them highly attractive for applications in functional materials and biomedicine. This comprehensive review presents an overview of the molecular characteristics, extraction and identification of ferritin, ferritin receptors, as well as the advancements in the directional design of high-order assemblies of ferritin and the applications based on its unique structural properties. Specifically, this Review focuses on the regulation of ferritin assembly from one to three dimensions, leveraging the symmetry of ferritin and modifications on key interfaces. Furthermore, it discusses targeted delivery of nutrition and drugs through facile loading and functional modification of ferritin. The aim of this Review is to inspire the design of micro/nano functional materials using ferritin and the development of nanodelivery vehicles for nutritional fortification and disease treatment.

show abstract

“…Chicken spleen ferritin has been characterized and its structure compared with horse ferritin (Shinjyo, 1973). More recently, the partial purification (Gonzalez del Barrio & Martin-Mateo, 1983) and the purification (Santos-Benito & Martin-Mateo, 1983) of chicken liver ferritin were also reported. In this report we describe the purification ofchicken liver ferritin by two novel methods: gel permeation chromatography over controlled-pore glass beads, and immunoaffinity chromatography using a monoclonal antibody specific for chicken ferritin.…”

Section: Introductionmentioning

confidence: 99%

Purification of chicken liver ferritin by two novel methods and structural comparison with horse spleen ferritin

Passaniti

Roth

1989

Biochemical Journal

View full text Add to dashboard Cite

Ferritin was purified from chicken liver by two different methods: gel filtration on controlled-pore glass beads, and immunoaffinity chromatography employing a chicken ferritin-specific monoclonal antibody that did not cross-react with horse spleen ferritin. This antibody recognizes intact ferritin and an oligomeric 240 kDa form of the molecule after protein transfer to nitrocellulose, but not the 22 kDa chicken ferritin subunit. Chicken liver ferritin purified by these methods exhibited reduced migration on non-denaturing polyacrylamide gels compared with horse spleen ferritin. These results were consistent with the difference in calculated isoelectric points of chicken and horse ferritin subunits. By two-dimensional gel electrophoresis, chicken ferritin 22 kDa subunits exhibited isoelectric points from 6.1 to 6.6 whereas horse spleen ferritin subunits exhibited isoelectric points of 5.8-6.3. The 240 kDa form of the chicken ferritin molecule had an isoelectric point of 6.6 whereas the 210 kDa form of the horse ferritin molecule had isoelectric points of 5.1 and 4.9. Intact chicken liver ferritin particles were 13.4 +/- 0.8 nm (controlled-pore glass-purified) and 12.5 +/- 0.9 nm (affinity-purified) in diameter when viewed by electron microscopy. Horse spleen ferritin consisted of slightly smaller particles with an average diameter of 11.0 +/- 0.7 nm. However, ferritin from chicken liver and horse spleen co-migrated with an apparent molecular mass of 470 kDa when analysed by Sepharose 4B gel filtration chromatography. These results indicate that, consistent with results from other published purification methods, the chicken ferritin purified by the methods reported here exhibits both structural similarities to, and differences from, horse spleen ferritin.

show abstract

Isolation, purification and characterization of spleen ferritin of Gallus domesticus L.

Cited by 8 publications

References 5 publications

Nuclear Ferritin: A Ferritoid-Ferritin Complex in Corneal Epithelial Cells

Nuclear Ferritin: A Ferritoid-Ferritin Complex in Corneal Epithelial Cells

Advancements of the Molecular Directed Design and Structure–Activity Relationship of Ferritin Nanocage

Purification of chicken liver ferritin by two novel methods and structural comparison with horse spleen ferritin

Contact Info

Product

Resources

About