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...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 116; no. 1; pp. 244 - 250
Main Authors Boyer, Rodney F., Schori, Barbara E.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 14.10.1983
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Summary: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.
Bibliography:ObjectType-Article-1
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(83)90407-2