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KMID : 0578319910010040439
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Molecules and Cells
1991 Volume.1 No. 4 p.439 ~ p.444
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Protein Carboxyl Methylation in Mitochondria, peroxisome and Lysosome of Rat Liver by Maturation
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Choi Hye-Jung
Jhon Gil-Ja
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Abstract
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Protein Methylation by protein carboxyl methyltransferase (EC 2.1.1.77) which has the specificity for the protein containing atypical aspartyl residues was investigated in mitochondria, peroxisome and lysosome of age-related rat liver. These subcellular organelles were separated by percoll density gradient centrifugation. The levels of the enzyme in three organelles increased by maturation and methyl accepting abilities also increased. The 19-, 30- and 38-kDa polypeptides in mitochondria and peroxisome and the 38-kDa one in lysosome were found to be the major endogenous substrates for this enzyme by cetylpyridium chloride-polyacrylamide gel electrophoresis and autoradiography. These results in the mitochondria, peroxisome, and lysosome of rat liver were consistent with that of brain cytosolic enzyme that participates in repair or degradation of age-dependent deamidated proteins.
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KEYWORD
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