The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi

Ferritins from the liver and spleen of the cold-adapted Antarctic teleosts Trematomus bernacchii and Trematomus newnesi have been isolated and characterized. Interestingly, only H- and M-chains are expressed and no L-chains. The H-chains contain the conserved ferroxidase center residues while M-chai...

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Bibliographic Details
Published in:Archives of Biochemistry and Biophysics
Main Authors: GIORGI, ALESSANDRA, MIGNOGNA, Giuseppina, GATTONI, Maurizio, CHIARALUCE, Roberta, CONSALVI, Valerio, CHIANCONE, Emilia, STEFANINI, Simonetta, Giuliano Bellapadrona
Other Authors: Giorgi, Alessandra, Mignogna, Giuseppina, Giuliano, Bellapadrona, Gattoni, Maurizio, Chiaraluce, Roberta, Consalvi, Valerio, Chiancone, Emilia, Stefanini, Simonetta
Format: Article in Journal/Newspaper
Language:English
Published: ELSEVIER SCIENCE INC, 360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA 2008
Subjects:
antarctic fish ferritin
cold adaptation
heteropolymeric assembly
trematomus bernacchii
trematomus newnesi
Antarctic
The Antarctic
Fish Point
Antarc*
Online Access:http://hdl.handle.net/11573/225586
https://doi.org/10.1016/j.abb.2008.06.022
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