Expression and structural and functional properties of human ferritin L-chain from Escherichia coli

Sonia Levi, Jochen Salfeld, Francesca Franceschinelli, Anna Cozzi, Marianne H. Dorner, Paolo Arosio

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Abstract

The human ferritin L-chain cDNA was cloned into a vector for overproduction in Escherichia coli, under the regulation of a λ promoter. The plasmid obtained contains the full L-chain coding region modified at the first two codons. It is able to direct the synthesis of the L-chain which can constitute up to 15% of the total soluble protein of bacterial extract. The L-chains assemble to form a ferritin homopolymer with electrophoretic mobility, molecular weight, thermal stability, spectroscopic, and immunological properties analogous to natural ferritin from human liver (95% L-chain). This recombinant L-ferritin is able to incorporate and retain iron in solution at physiological pH values. At variance with the H-ferritin, the L form does not uptake iron at acidic pH values and does not show detectable ferroxidase activity. It is concluded that ferritin L-chain lacks the ferroxidase site present in the H-chain and that the two chains may have specialized functions in intracellular iron metabolism.

Original languageEnglish
Pages (from-to)5179-5184
Number of pages6
JournalBiochemistry
Volume28
Issue number12
Publication statusPublished - 1989

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Levi, S., Salfeld, J., Franceschinelli, F., Cozzi, A., Dorner, M. H., & Arosio, P. (1989). Expression and structural and functional properties of human ferritin L-chain from Escherichia coli. Biochemistry, 28(12), 5179-5184.