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

FEBS Letters

Levi, Sonia²  Santambrogio, Paolo²  Albertini, Alberto¹  Arosio, Paolo² 

[1] Institute of Chemistry, University of Brescia, Via Valsabbina, Brescia, Italy;DIBIT, San Raffaele Scientific Institute, Department of Biomedical Science and Technology, University of Milano, Via Olgettina 58, 20132 Milano, Italy

关键词: Ferroxidase;    Ferritin;    Iron protein;    Protein assembly;    GdnHCl;    guanidine hydrochloride;    DTT;    dithiothreitol;    CD;    circular dichroism;    rHF;    recombinant human H-chain ferritin;    rLF;    recombinant human L-chain ferritin;   

DOI  :  10.1016/0014-5793(93)80826-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown