Elemental iron is required for a variety of normal cellular functions and vital for proper growth and development.
Iron absorption occurs primarily in the intestine (duodenum) and inversely related to body iron reserve.
Several proteins including Ferritin, transferrin (Tf), transferrin receptors (TfRs), and iron regulatory proteins (IRPs) etc play a key role in iron metabolism.
Ferritin is the major protein involved in iron sequestration and detoxification.
Ferritin is found in all living species and its three dimensional structure is conserved in all species despite very low sequence identity from bacteria to human.
Mammalian liver and spleen ferritin (~450kD) consists of 24 subunits of 2 species, the heavy subunit (~21kD; FTH) and the light subunit (~ 19kD; FTL).
The 2 types of apoferritin subunits were designated H and L for heart and liver, respectively.
Ferritin molecules from plants and bacteria contain only H-type chains, where 'H-type' is associated with the presence of centers catalyzing the oxidation of two Fe(II) atoms.
FTL subunit (rich in human liver and spleen) is coded by a gene in segment 19q13.3 and FTH subunit (rich in human heart) is located on chromosome 11.
Ferritin is capable of storing up to 4,500 atoms of ferric iron.
The H-to-L ratio within ferritin varies in a tissue-specific manner and is also influenced by pathophysiological conditions, including inflammation and malignancy.
H-chains are important for Fe(II) oxidation and Lchains assist in core formation.
Applications:Suitable for use in ELISA.
Western Blot, though not tested, may potentially be used as an application.
