Abstract
Actin was purified to apparent homogeneity from the matrix of ultra-pure mitochondria of rat livers by DNase-I affinity chromatography and HPLC gel filtration. The mitochondrial actin was immunologically identified by an anti-actin antibody, and its apparent molecular weight was 43 KDa, as determined by SDS-polyacrylamide gel electrophoresis. The immunohistochemical study revealed the localization of the mitochondrial actin in the matrix space and on the internal surface of inner membrane. The actin fraction eluted from a DNase-I column by KC1-EGTA solution underwent polymerization and bundling in vitro.
| Original language | English |
|---|---|
| Pages (from-to) | 599-606 |
| Number of pages | 8 |
| Journal | Biochemistry International |
| Volume | 20 |
| Issue number | 3 |
| Publication status | Published - 1990 |
ASJC Scopus subject areas
- Biochemistry