Abstract
Ferritin present within siderosomes of iron-loaded rats has a faster anodal mobility than that of cytosolic ferritin from the same rats. A 19-amino-acid-residue peptide was isolated from this fast ferritin and shown to be derived from the C-terminal end of its L-subunit. A 17.3 kDa peptide seen on electrophoresis in denaturing gels of this ferritin accounts for the major portion of the original 182-residue subunit. The two peptides arise from cleavage within the 'insertion region' of the L-subunit sequence that occurs between the D and E helices and lies on the outside of the assembled molecule. This cleavage is present in about 80% of the L-subunits of siderosomal ferritin but nevertheless leaves the molecular structure otherwise intact. It gives rise to an apparent decrease in molecular size, accounting for the faster anodal mobility on native gels. Hence a new form of heterogeneity in ferritin preparations has been explained.