Ferritin amino acid sequences

Table 6.1 Amino-acid sequence alignment of four mammalian ferritins (Horse L chain, HoL Human L chain, HuL Human H chain, HuH Rat H, RaH) and of one of the ferritins, FTN, and the bacterioferritin, BFR of...

Dimeric, trlmeric, and tetramerlc Interactions of ferritin subunits each have distinctive features which may relate to the function of the protein coat. Among vertebrates, at least, the amino acid sequence In such regions Is highly conserved, and forms structures which may have functional roles. 

Ferritin, 36 449-451, 43 363, 399-400 amino acid sequences, 36 465-467 bacterial, see Bacfer biochemistry, 36 450-451 dimer and larger cluster formation, 36 479-481... 

Table 15-1 Percentage amino acid sequence identities (excluding gaps) of aligned sequences of ferritins and rubrerythrin...

The best-studied ferritins are those from animal sources and these will be discussed first here. The subunits have relative masses of around 20,000 Da and turn out to come in two different forms distinguished as heavy (H) and light (L) with about 54% homology in amino acid sequence between the two. The H L ratio depends on the tissue of origin with more H subunits (about 2/3)... 

CE has proven to be useful in characterizing different molecular forms of various metalloproteins like metal-lothionein, transferrin, and conalbumin. Molecular forms arise from differences in the amino acid sequence of proteins (isoforms), differences in the amount or type of metal bound (metalloforms), or from differences in the type and amount of carbohydrate side chains linked to the protein (glycoforms). CZE was used to follow the formation of the oligomeric iron core and its incorporation into ferritin, to detect and quantify ferritin species or ferritin subunit proteins in purified or partially purified states, and to study the interaction of different metal ions with ferritin. 

Although they show little overall sequence identity, the dinuclear centers of the three prototype ferritins, particularly that of EcBfr, are remarkably similar in both amino acid residues and their geometry to those of the class 2 diiron proteins that comprises the ribonucleotide reductase R2 subunit (RNR R2), the methane monooxygenase hydroxylase component (MMOH), rubrerythrin (Rr) and several other... 

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