Ferritin from the spleen of the Anctartic teleost Trematomus bernacchii is an M-type homopolymer
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 a...
Published in: | European Journal of Biochemistry |
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Main Authors: | , , , , , |
Other Authors: | , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
BLACKWELL PUBLISHING LTD, 9600 GARSINGTON RD, OXFORD OX4 2DG, OXON, ENGLAND
2002
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Subjects: | |
Online Access: | http://hdl.handle.net/11573/251998 https://doi.org/10.1046/j.1432-1327.2002.02762.x http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000174575200002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-0036231083&partnerID=65&md5=03fcce759764aa678281739a728344b3 |
Summary: | 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). |
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