Tool for the study of protein synthesis and regulatory mechanisms.
Ferritin from human liver has been used as model protein in size-exclusion high-performance liquid chromatography technique and for synthetic nanopore translocation studies. It has also been used to test its effect on the susceptibility of shrimp (Litopenaeus vannamei) to the white spot syndrome virus.
Ferritin, cationized from horse spleen has been used:
- to incubate amoebae (106) in the study, to determine whether trophozoites are able to take up ferritin and internalise this protein for their growth in axenic culture
- to determine phagosome-lysosome fusion by electron microscopy
- to label freshly excised chick optic tecta in serum free incubation medium
FERRITIN, HUMAN is a major iron storage protein found in the spleen, liver and intestinal mucosa of vertebrates. It consists of a protein shell surrounding a crystalline, hydrated iron oxide-phosphate core.
Ferritin, an iron-storage protein is usually present in the liver and spleen in mammals. Iron and?ferritin?are distributed relatively same in the eye. Ferritin is made up of heavy and light chains.
Ferritin holds iron at its ferric state (Fe3+). The core of ferritin?has the capability to hold 4500 iron molecules. It is essential to store iron in vertebrates. Ferritin?is also essential to store and transport iron in invertebrates. It plays a key role in dietary iron absorption.
The purification of this major iron-binding protein is achieved by homogenisation in water and precipitation with ammonium sulfate, repeating the cycle of ultracentrifugation, and molecular sieve chromatography through a Sephadex 4B column. Isoelectric focusing reveals a broad spectrum of impurities which can be separated by ion-exchange chromatography on Sephadex A-25 and stepwise elution. [Konijn et al. Anal Biochem 144 423 1985.]
