The incorporation of iron into apoferritin as mediated by ceruloplasmin.
Ceruloplasmin, a copper ferroxidase, promotes the incorporation of Fe(III) into the iron storage protein, apoferritin. The product formed is identical to ferritin as judged by polyacrylamide electrophoresis and iron/protein measurements. Of several proteins examined, only apoferritin accumulates the Fe(III) produced by ceruloplasmin. When ceruloplasmin was replaced by tyrosinase, which we have shown to have ferroxidase activity, no iron incorporation into apoferritin was observed. It is proposed that Fe(III) is transferred directly and specifically to apoferritin. These data support a more specific role for ceruloplasmin in iron metabolism than has previously been proposed.
D001052:Apoferritins / Q000378:metabolism*; D001204:Ascorbate Oxidase / Q000378:metabolism; D002570:Ceruloplasmin / Q000502:physiology*; D005290:Ferric Compounds / Q000378:metabolism; D005293:Ferritins / Q000031:analogs & derivatives*; D005296:Ferrous Compounds; D006801:Humans; D007501:Iron / Q000378:metabolism*; D014442:Monophenol Monooxygenase / Q000378:metabolism
D005290:Ferric Compounds; D005296:Ferrous Compounds; D005293:Ferritins; D001052:Apoferritins; D007501:Iron; D001204:Ascorbate Oxidase; D014442:Monophenol Monooxygenase; D002570:Ceruloplasmin