The monomers and oligomers of ferritin and apoferritin: association and dissociation.
We have reinvestigated the association and dissociation of ferritin and apoferritin in phosphate buffer (pH 7.2, I = 0.05). When oligomer-enriched solutions of horse spleen ferritin were mixed with more concentrated, but unenriched solutions of horse spleen apoferritin, there was dissociation of the ferritin oligomers, as determined by polyacrylamide gel electrophoresis and from iron/protein ratios. Some evidence was also obtained for association of monomers in the mixture of ferritin and apoferritin after pelleting and redissolution of pellets in minimal volumes of the phosphate buffer. Monomer-enriched, biosynthetically labeled rat liver ferritin was pelleted, redissolved in minimal volumes of phosphate buffer, and separated by polyacrylamide gel electrophoresis; the fractions were isolated and counted. The results revealed that an association of monomers of the rat liver ferritin had taken place which doubled the concentration of dimers. However, our results also indicate that association by concentration was limited to a fraction of monomers.
D000818:Animals; D001052:Apoferritins; D001665:Binding Sites; D004589:Electrophoresis, Disc; D005293:Ferritins / Q000031:analogs & derivatives*; D006736:Horses; D007501:Iron / Q000032:analysis; D008099:Liver / Q000032:analysis; D046911:Macromolecular Substances; D009928:Organ Specificity; D010710:Phosphates; D011485:Protein Binding; D051381:Rats; D013045:Species Specificity; D013154:Spleen / Q000032:analysis
D046911:Macromolecular Substances; D010710:Phosphates; D005293:Ferritins; D001052:Apoferritins; D007501:Iron