A new form of ferritin heterogeneity explained. Isolation and identification of a nineteen-amino-acid-residue fragment from siderosomal ferritin of rat liver.

@article{Andrews1987ANF,
  title={A new form of ferritin heterogeneity explained. Isolation and identification of a nineteen-amino-acid-residue fragment from siderosomal ferritin of rat liver.},
  author={Simon C Andrews and Amyra Treffry and Pauline M. Harrison},
  journal={The Biochemical journal},
  year={1987},
  volume={245 2},
  pages={447-53}
}
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… CONTINUE READING

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