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

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