Relative in vitro stability of ornithine decarboxylase from liver preneoplastic nodules and hepatomas.
A very rapid and drastic microsome-dependent in vitro inactivation of the hydrocortisone-induced ornithine decarboxylase in rat liver was reported recently (M. F. Zuretti and E. Gravela, Biochim. Biophys. Acta. 742: 269-277, 1983). Present results show that ornithine decarboxylase from preneoplastic nodules and hepatomas, which have been induced in rats by N-2-fluorenylacetamide, is much more stable, its greater stability not being accounted for by a lower microsome-bound inactivating capacity. The possibility of a relationship between the in vitro enzyme stability and the increase of enzyme activity in neoplastic tissues is suggested.
D015073:2-Acetylaminofluorene; D000818:Animals; D001711:Biotransformation; D002262:Carboxy-Lyases / Q000378:metabolism*; D008113:Liver Neoplasms / Q000139:chemically induced / Q000201:enzymology*; D008114:Liver Neoplasms, Experimental / Q000139:chemically induced / Q000201:enzymology*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D009955:Ornithine Decarboxylase / Q000378:metabolism*; D011230:Precancerous Conditions / Q000139:chemically induced / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains
D015073:2-Acetylaminofluorene; D002262:Carboxy-Lyases; D009955:Ornithine Decarboxylase