Mouse kidneys were perfused with Krebs-Ringer bicarbonate buffer (KRB) containing native, anionic horse spleen ferritin or various cationized derivatives, and the glomerular localization of the probe molecules determined by electron microscopy. Ferritins cationic with respect to the medium (KRB, pH 7.45) accumulated in the subendothelial layers of the glomerular basement membrane (GBM) in amoun...

Ferritins are iron-storage proteins that accumulate in plastids during seed formation, and also in leaves during senescence or iron overload. Iron release from ferritins occurs during growth of seedlings and greening of plastids. Depending on the concentration of the reducing agent ascorbate, either an overall iron release or uptake by ferritins from iron(III) citrate may occur. We have designe...

Ferritin is a nanocage protein made of 24 subunits. Its major role is to manage intracellular concentrations of free Fe(ii) and Fe(iii) ions, which is pivotal for iron homeostasis across all domains of life. This function of the protein is regulated by a conserved di-iron catalytic center and has been the subject of extensive studies over the past 50 years. Yet, it has not been fully understood...

Bioiron - central to respiration, photosynthesis and DNA synthesis and complicated by radical chemistry with oxygen - depends on ferritin, the super family of protein nanocages (maxi-ferritins in humans, animals, plant, and bacteria, and mini-ferritins, also called DPS proteins, in bacteria) for iron and oxygen control. Regulation of ferritin synthesis, best studied in animals, uses DNA transcr...

Ferritin is the iron-storage protein of eukaryotic organisms. The nucleotide sequence encoding Azotobacter vinelandii bacterioferritin, a hemoprotein, was determined. The deduced amino acid sequence reveals a high degree of identity with Escherichia coli bacterioferritin and a striking similarity to eukaryotic ferritins. Moreover, derivation of a global alignment shows that virtually all key re...

The iron storage protein ferritin is the principal yolk protein in oocytes of the snails Planorbarius corneus L. and Lymnaea stagnalis L. This report gives an account of the isolation procedure and of some properties of snail ferritins. The isolation procedure includes a heat-denaturation step, gel filtration on Sepharose 6B and two ultracentrifugation steps followed by electrophoresis. Ferriti...

1. Horse spleen ferritin and human liver ferritin were examined by gel electrofocusing under conditions that demonstrated equilibrium focusing. Both ferritins were resolved into multiple isoferritins. Both families of isoferritins were separable from one another. 2. Horse spleen ferritin was also resolved into five components by ion-exchange chromatography on DEAE-Sephadex A-50. Each of the maj...