Isolation, purification and characterization of bovine spleen ferritin |
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Authors: | N Cetinkaya F W Lengemann P Kogan |
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Abstract: | 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. |
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