Ferritin: Difference between revisions
Jump to navigation
Jump to search
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
Line 9: | Line 9: | ||
* '''Thioferritin''' (TFR) is a ferritin-related protein with 2 cysteine residues adjacent to the dimetal binding site.<br /> | * '''Thioferritin''' (TFR) is a ferritin-related protein with 2 cysteine residues adjacent to the dimetal binding site.<br /> | ||
* '''DNA-binding Protein of Starved cells''' (Dps) - a ferritin-like diiron carboxylate.<br /> | * '''DNA-binding Protein of Starved cells''' (Dps) - a ferritin-like diiron carboxylate.<br /> | ||
== Relevance == | == Relevance == |
Revision as of 09:24, 23 June 2024
FunctionFerritin (FR) is an iron storage and release protein. It stores iron as microcrystals with phosphate and hydroxide ions. FR is composed of 24 subunits of heavy chain (FTH) and light chain (FTL).[1] Amphibians have an additional middle subunit FR (FTM).
RelevanceCavities formed by FR are used for the manufacture of nanoparticles. FR is used as a marker for iron overload disorder. DiseaseFR deficiency can lead to anemia. 3D Structures of Ferritin
|
|
ReferencesReferences
- ↑ Wang W, Knovich MA, Coffman LG, Torti FM, Torti SV. Serum ferritin: Past, present and future. Biochim Biophys Acta. 2010 Aug;1800(8):760-9. doi: 10.1016/j.bbagen.2010.03.011. , Epub 2010 Mar 19. PMID:20304033 doi:http://dx.doi.org/10.1016/j.bbagen.2010.03.011