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

Journal Article · Tue Jun 13 00:00:00 EDT 1989 · Biochemistry; (USA)

DOI:https://doi.org/10.1021/bi00438a040· OSTI ID:5353494

Levi, S; Salfeld, J; Franceschinelli, F; Cozzi, A; Dorner, M H; Arosio, P ^[1]

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1. Univ. of Milan (Italy)

The human ferritin L-chain cDNA was cloned into a vector for overproduction in Escherichia coli, under the regulation of a {lambda} 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.

• OSTI ID: 5353494
• Journal Information: Biochemistry; (USA), Vol. 28:12; ISSN 0006-2960
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
METALLOPROTEINS
MOLECULAR STRUCTURE
RECOMBINANT DNA
DNA-CLONING
CODONS
ELECTROPHORESIS
ESCHERICHIA COLI
FERRITIN
HEART
LIVER
PH VALUE
PLASMIDS
PURIFICATION
BACTERIA
BODY
CARDIOVASCULAR SYSTEM
CELL CONSTITUENTS
CLONING
COMPLEXES
DIGESTIVE SYSTEM
DNA
DNA HYBRIDIZATION
GLANDS
HYBRIDIZATION
IRON COMPLEXES
MICROORGANISMS
NUCLEIC ACIDS
ORGANIC COMPOUNDS
ORGANS
PROTEINS
TRANSITION ELEMENT COMPLEXES
550201* - Biochemistry- Tracer Techniques