[Intramitochondrial proteolytic activity of rat liver].
Highly purified mitochondria and lysosomes are isolated from rat liver homogenate. pH optimum of proteolytic activity with respect to proteins of own structures and to mitochondrial structural protein is investigated. The purification of mitochondria from lysosomes is found to be accompanied by the change of proteolytic activity pH optimum from 5.0 to 6.0 in coarse and purified mitochondria respectively. Comparative study of structural protein hydrolysis products with enzyme preparations from purified mitochondria and lysosomes has revealed differences in the spectrum of the reaction products. The data obtained suggest a presence of a proteolytic enzyme in rat liver mitochondria.
D000818:Animals; D002458:Cell Fractionation; D005260:Female; D006863:Hydrogen-Ion Concentration; D008247:Lysosomes / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D051381:Rats
D010447:Peptide Hydrolases
Vnutrimitokhondrial'naia proteoliticheskaia aktivnost' pecheni krys.