Aging changes in intracellular protein breakdown.
Using radioactively labelled cytosol proteins as substrates we were able to exclude the possible accumulation of any specific inhibitor for the lysosomal proteases in rat liver cytosol during the aging process. There were also no gross changes in the molecular weight patterns of these proteins during the aging process. The percentage of more hydrophobic proteins seems to be identical in both the "old" and "young" cytosol proteins. From immunological experiments we suppose a qualitative change in the composition of rat liver cytosol proteins or of their properties during the aging process.
D000375:Aging; D000818:Animals; D003600:Cytosol / Q000378:metabolism; D007123:Immunoelectrophoresis, Two-Dimensional; D008099:Liver / Q000254:growth & development* / Q000378:metabolism; D008247:Lysosomes / Q000201:enzymology; D010447:Peptide Hydrolases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D051381:Rats
D011506:Proteins; D010447:Peptide Hydrolases