Open Accessl ‐Ornithine‐induced inactivation of mammalian ornithine decarboxylase in vitro
Author(s) -
DANZIN Charles,
PERSSON Lo
Publication year - 1987
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1987.tb13481.x
Subject(s) - ornithine decarboxylase , spermidine , ornithine , putrescine , ornithine decarboxylase antizyme , spermine , dithiothreitol , biochemistry , chemistry , thioacetamide , in vitro , enzyme , biology , microbiology and biotechnology , arginine , amino acid
Partially purified ornithine decarboxylase, isolated from the liver of thioacetamide‐treated rats, is stable in the absence of added low‐molecular‐mass thiols or other reducing agents. However, under these conditions, the enzyme is rapidly inactivated upon incubation with l ‐ornithine or l ‐2‐methylornithine. The inactivation process follows first‐order kinetics, and saturation kinetics are observed. Rapid recovery of activity is observed after subsequent addition of dithiothreitol. As distinct from L‐ornithine, d ‐ornithine, putrescine, spermidine, or spermine do not produce inactivation of ornithine decarboxylase. Very similar results are obtained with pure ornithine decarboxylase isolated from androgen‐stimulated mouse kidney, stabilized with a rat liver extract.