Human ferritin H-chains can be obtained in non-assembled stable forms which have ferroxidase activity

Sonia Levi, Paolo Santambrogio, Alberto Albertini, Paolo Arosio

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

We found conditions to obtain the Leu-169 → Arg mutant of human ferritin H chain in a stable and non-assembled state. The protein obtained is an oligomer of subunits with a high degree of structured conformation, and when concentrated it re-assembles into ferritin cages. Functional studies showed that (i) it promotes iron oxidation like the assembled ferritin, but at slower rate, (ii) it is readily precipitated by the oxidised iron unless apotransferrin or L-chain ferritin are added to sequester Fe(III). The results confirm that ferroxidase activity is located within the H-chain, and indicate that the cages of the fully assembled ferritins are important not only in maintaining iron in a soluble form, but also in eliciting the activity of the ferroxidase centres.

Original languageEnglish
Pages (from-to)309-312
Number of pages4
JournalFEBS Letters
Volume336
Issue number2
DOIs
Publication statusPublished - Dec 27 1993

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Apoferritins
Ceruloplasmin
Ferritins
Iron
Oligomers
Conformations
Oxidation
Proteins

Keywords

  • Ferritin
  • Ferroxidase
  • Iron protein
  • Protein assembly

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Human ferritin H-chains can be obtained in non-assembled stable forms which have ferroxidase activity. / Levi, Sonia; Santambrogio, Paolo; Albertini, Alberto; Arosio, Paolo.

In: FEBS Letters, Vol. 336, No. 2, 27.12.1993, p. 309-312.

Research output: Contribution to journalArticle

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