Release of acid proteolytic activity from lysosomes and degradation of protein in organs of rats intoxicated with ethanol and acetaldehyde.
Intoxication with ethanol and acetaldehyde resulted in a marked increase of the acid proteolytic activity in the post-lysosomal supernatant of rat kidney, lung, and liver, while the content of protein and acid-soluble tyrosine remained practically unchanged. Proteins of the post-lysosomal supernatant were degraded in vitro by the endogenous proteinase(s) of lysosomal origin at pH 3.5 and 5.5 but not at pH 7.0.
D000079:Acetaldehyde / Q000633:toxicity*; D000435:Alcoholic Intoxication / Q000201:enzymology*; D000818:Animals; D007668:Kidney / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D008168:Lung / Q000201:enzymology; D008247:Lysosomes / Q000201:enzymology*; D017830:Octoxynol; D010447:Peptide Hydrolases / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000494:pharmacology; D011506:Proteins / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013997:Time Factors
D011506:Proteins; D011092:Polyethylene Glycols; D017830:Octoxynol; D010447:Peptide Hydrolases; D000079:Acetaldehyde