Purification and immunohistochemical study of actin in mitochondrial matrix

S. Etoh, H. Matsui, M. Tokuda, T. Itano, M. Nakamura, O. Hatase

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)


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 languageEnglish
Pages (from-to)599-606
Number of pages8
JournalBiochemistry International
Issue number3
Publication statusPublished - 1990

ASJC Scopus subject areas

  • Biochemistry


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