We have compared the size and shape of ferritins from human heart, rat heart, and skeletal muscle with those of rat liver and horse spleen ferritins, using sedimentation and gel filtration techniques. The electrophoretically "fast" form of heart ferritin was partially separated from both the "slow" heart form and from rat liver ferritin by gel filtration (Stokes radii 72 A versus 69 and 68.5 A)...

Serum ferritin has been used widely in clinical medicine chiefly as an indicator of iron stores and inflammation. Circulating ferritin also can have paracrine effects. Despite the clinical significance of serum ferritin, its secretion remains an enigma. The consensus view is that serum ferritin arises from tissue ferritins--principally ferritin light--which can be glycosylated. Ferritin heavy a...

Ferritins and bacterioferritins are iron storage proteins that represent key players in iron homeostasis. Several organisms possess both forms of ferritins, however, their relative physiological roles are less understood. Mycobacterium tuberculosis possesses both ferritin (BfrB) and bacterioferritin (BfrA), playing an essential role in its pathogenesis as reported by us earlier. This study prov...

Ferritin from Reuber H-35 hepatomas was compared with ferritin from livers of ACI rats, the strain of rats in which the original H-35 hepatoma developed. The isoelectric points of these two proteins are 5.20 ±0.02 (H-35 ferritin) and 4.95 ±0.03 (ACI liver ferritin). The amino acid composition of apoferritin prepared from H-35 hepatoma ferritin differs significantly from that of ACI rat liver ...

Bacterial and mammalian ferritins are known to bind heme. The use of α-casein and biotinylated hemin could be applicable to detection of protein-bound heme and of proteins with heme-binding capacity, respectively. Although commercial horse spleen ferritin and purified horse spleen ferritin (L:H subunit ratio=4) bound to an α-casein-coated plate, and this binding could be inhibited by hemin, rec...

Serum ferritin has been used widely in clinical medicine chiefly as an indicator of iron stores and inflammation. Circulating ferritin also can have paracrine effects. Despite the clinical significance of serum ferritin, its secretion remains an enigma. The consensus view is that serum ferritin arises from tissue ferritins— principally ferritin light—which can be glycosylated. Ferritin heavy an...

Background and aims: Iron is stored in hepatocytes in the form of ferritin and haemosiderin. There is a marked increase in iron rich haemosiderin in iron overloaded livers, and ferric iron in amounts exceeding the ferritin and haemosiderin binding capacity may promote free radical generation, causing cellular damage. The aim of this study was to characterise hepatic haemosiderin using four anti...

Ticks are obligate hematophagous parasites and important vectors of diseases. The large amount of blood they consume contains great quantities of iron, an essential but also toxic element. The function of ferritin, an iron storage protein, and iron metabolism in ticks need to be further elucidated. Here, we investigated the function a newly identified secreted ferritin from the hard tick Haemap...

Ferritin from Reuber H-35 hepatomas was compared with ferritin from livers of ACI rats, the strain of rats in which the original H-35 hepatoma developed. The isoelectric points of these two proteins are 5.20 ±0.02 (H-35 ferritin) and 4.95 ±0.03 (ACI liver ferritin). The amino acid composition of apoferritin prepared from H-35 hepatoma ferritin differs significantly from that of ACI rat liver ...

Ferritins are protein nanocages that accumulate inside their cavity thousands of oxidized iron atoms bound to oxygen and phosphates. Both characteristic types of eukaryotic ferritin subunits are present in secreted ferritins from insects, but here dimers between Ferritin 1 Heavy Chain Homolog (Fer1HCH) and Ferritin 2 Light Chain Homolog (Fer2LCH) are further stabilized by disulfide-bridge in th...