Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 1363-1369 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 148 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Nov 13 1987 |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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Protein heterogeneity in rabbit liver ferritin : Two types of molecular dimers. / Santambrogio, Paolo; Massover, William H.
In: Biochemical and Biophysical Research Communications, Vol. 148, No. 3, 13.11.1987, p. 1363-1369.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Protein heterogeneity in rabbit liver ferritin
T2 - Two types of molecular dimers
AU - Santambrogio, Paolo
AU - Massover, William H.
PY - 1987/11/13
Y1 - 1987/11/13
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0023652799&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0023652799&partnerID=8YFLogxK
U2 - 10.1016/S0006-291X(87)80282-6
DO - 10.1016/S0006-291X(87)80282-6
M3 - Article
C2 - 3120715
AN - SCOPUS:0023652799
VL - 148
SP - 1363
EP - 1369
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -