Ferritin subunits in livers of siderotic mice.
The major ferritin species of mouse liver has been resolved by SDS-PAGE into two bands similar to the H and L subunits of rat liver ferritin with the L subunit predominating. Amino acid sequencing has confirmed the major, faster-migrating component as L chain. An additional, electrophoretically fast, minor ferritin was isolated from siderosome-containing subcellular fractions. In denaturing gels it gave a single 'F' subunit band of about 17 kDa, significantly smaller than the L and H subunits (about 20 and 21 kDa respectively). A small fragment isolated from the fast ferritin was sequenced. It corresponds to a 19-residue C-terminal peptide cleaved from L subunits in the assembled molecules. The F subunit must be derived from L subunits by loss of this peptide, and is not the expression product of a different gene. 'Fast' ferritins of siderotic mice and rats are thus analogous.
Dean
B
B
Department of Molecular Biology and Biotechnology, University, Sheffield, UK.
Andrews
S C
SC
Treffry
A
A
Harrison
P M
PM
Keen
J N
JN
Findlay
J B
JB
D000595:Amino Acid Sequence; D000818:Animals; D001052:Apoferritins / Q000302:isolation & purification; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005293:Ferritins / Q000302:isolation & purification / Q000378:metabolism*; D008099:Liver / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D012806:Siderosis / Q000378:metabolism*
D005293:Ferritins; D001052:Apoferritins; D003488:Cyanogen Bromide