Abstract
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.
Footnotes
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↵1 Present work was supported by Associazione Italiana per la Ricerca sul Cancro and by the National Foundation for Cancer Research, Turin's Workshop.
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↵2 To whom requests for reprints should be addressed, at Patologia Generale, Corso Raffaello 30, 10125 Torino, Italy.
- Received July 22, 1982.
- Accepted February 3, 1983.
- ©1983 American Association for Cancer Research.
Volume 43, Issue 5
