Ferritin from the spleen of the Antarctic teleost Trematomus bernacchii is composed of a single subunit that contains both the ferroxidase center residues, typical of mammalian H chains, and the carboxylate residues forming the micelle nucleation site, typical ofmammalianL chains.Comparison of the amino-acid sequence with those available from lower vertebrates indicates that T. bernacchii ferritin can be classi®ed as an M-type homopolymer. Interestingly, the T. bernacchii ferritin chain shows 85.7% identity with a cold- inducible ferritin chain of the rainbow trout Salmo gairdneri. The structural and functional properties indicate that cold acclimation and functional adaptation to low temperatures are achieved without signi®cant modi®cation of the protein stability. In fact, the stability of T. bernacchii ferritin to de- naturation induced by acid or temperature closely resembles that of mesophilic mammalian ferritins. Moreover iron is taken up e ciently and the activation energy of the reaction is 74.9 kJámol)1, a value slightly lower than that measured for the human recombinant H ferritin (80.8 kJámol)1).

Ferritin from the spleen of the Anctartic teleost Trematomus bernacchii is an M-type homopolymer / Mignogna, Giuseppina; Chiaraluce, Roberta; Consalvi, Valerio; Cavallo, Stefano; Stefanini, Simonetta; Chiancone, Emilia. - In: EUROPEAN JOURNAL OF BIOCHEMISTRY. - ISSN 0014-2956. - STAMPA. - 269:(2002), pp. 1600-1606. [10.1046/j.1432-1327.2002.02762.x]

Ferritin from the spleen of the Anctartic teleost Trematomus bernacchii is an M-type homopolymer

MIGNOGNA, Giuseppina;CHIARALUCE, Roberta;CONSALVI, Valerio;CAVALLO, Stefano;STEFANINI, Simonetta;CHIANCONE, Emilia
2002

Abstract

Ferritin from the spleen of the Antarctic teleost Trematomus bernacchii is composed of a single subunit that contains both the ferroxidase center residues, typical of mammalian H chains, and the carboxylate residues forming the micelle nucleation site, typical ofmammalianL chains.Comparison of the amino-acid sequence with those available from lower vertebrates indicates that T. bernacchii ferritin can be classi®ed as an M-type homopolymer. Interestingly, the T. bernacchii ferritin chain shows 85.7% identity with a cold- inducible ferritin chain of the rainbow trout Salmo gairdneri. The structural and functional properties indicate that cold acclimation and functional adaptation to low temperatures are achieved without signi®cant modi®cation of the protein stability. In fact, the stability of T. bernacchii ferritin to de- naturation induced by acid or temperature closely resembles that of mesophilic mammalian ferritins. Moreover iron is taken up e ciently and the activation energy of the reaction is 74.9 kJámol)1, a value slightly lower than that measured for the human recombinant H ferritin (80.8 kJámol)1).
2002
01 Pubblicazione su rivista::01a Articolo in rivista
Ferritin from the spleen of the Anctartic teleost Trematomus bernacchii is an M-type homopolymer / Mignogna, Giuseppina; Chiaraluce, Roberta; Consalvi, Valerio; Cavallo, Stefano; Stefanini, Simonetta; Chiancone, Emilia. - In: EUROPEAN JOURNAL OF BIOCHEMISTRY. - ISSN 0014-2956. - STAMPA. - 269:(2002), pp. 1600-1606. [10.1046/j.1432-1327.2002.02762.x]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/251998
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