Isolation, purification and characterization of bovine spleen ferritin.

Ferritin was isolated from bovine spleen and used to prepare apoferritin and reconstituted ferritin. The mol. wt of bovine ferritin was 464,000 with monomer subunits about 18,000-19,500. Gel electrophoresis showed three bands each for ferritin, apoferritin and reconstituted ferritin; all stained for protein and carbohydrate. Only apoferritin failed to stain for iron. Bovine ferritin had higher concentrations of proline, threonine, and valine than equine or human ferritin. The iron:protein ratio of bovine ferritin was 0.161 and of equine ferritin was 0.192. After iron uptake by the apoferritins the iron:protein ratios were 0.186 and 0.278 for the bovine and equine ferritins, respectively.