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Purification and immunohistochemical study of actin in mitochondrial matrix
Authors:S Etoh  H Matsui  M Tokuda  T Itano  M Nakamura  O Hatase
Institution:Department of Physiology, Kagawa Medical School, Japan.
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 KCl-EGTA solution underwent polymerization and bundling in vitro.
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