Isolation and characterization of human liver cell actin and 53 K dalton protein.
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We prepared and characterized human liver cell actin and its properties. Crude actin fraction was extracted from acetone powder of isolated liver cells, obtained from 5 autopsy cases without liver diseases. Actin was purified by specific binding with rabbit skeletal myosin followed by dissociation with Mg-ATP. Purified fraction contained 42 K protein and 53 K protein. Actin was also purified from crude fraction using DNase-I affinity column chromatography. 42 K protein was eluted at 3.0M guanidine-HCl and 53 K protein at 0.75M. These proteins were separated by preparative gel electrophoresis and characterized. Biochemical and ultrastructural studies strongly indicate that the 42 K protein is actin. 53 K protein copurified with actin, thus suggesting interaction of the two proteins.
- 社団法人 日本肝臓学会の論文
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