Purification and immunohistochemical study of actin in mitochondrial matrix.
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.
Etoh
S
S
Department of Physiology, Kagawa Medical School, Japan.
Matsui
H
H
Tokuda
M
M
Itano
T
T
Nakamura
M
M
Hatase
O
O
D000199:Actins / Q000032:analysis / Q000302:isolation & purification*; D000818:Animals; D001704:Biopolymers; D002499:Centrifugation, Density Gradient; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D003850:Deoxyribonuclease I; D015151:Immunoblotting; D008854:Microscopy, Electron; D008930:Mitochondria, Liver / Q000032:analysis*; D051381:Rats; D011919:Rats, Inbred Strains; D013367:Submitochondrial Particles / Q000032:analysis*
D000199:Actins; D001704:Biopolymers; D003850:Deoxyribonuclease I