Native pore-gradient polyacrylamide gel electrophoresis of rabbit liver ferritin reveals the usual single band of molecular monomers, but shows two bands at the position of molecular dimers. The proteins in these three bands were purified by excision from preparative slab gels. All three bands (1) contain considerable amounts of iron-rich ferritin when examined by electron microscopy, (2) show complete identity when reacted with antirabbit-ferritin antibodies, and (3) have similar amounts of H-type and L-type ferritin subunits with denaturing polyacrylamide gel electrophoresis. These results establish that there are two classes of ferritin molecular dimers. The larger diner band uniquely also contains a polypeptide with Mr = 170,000. This unusual type of ferritin heterogeneity seems to be due to the presence of a non-ferritin protein associated only with one class of dimers.
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - Nov 13 1987|
ASJC Scopus subject areas
- Molecular Biology