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Updated: Oct 20, 2026
Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
Published on: November 23, 2016
Identical catalytic-centre activity for mouse kidney and rat liver ornithine decarboxylases as determined with
M Marumo1, S Matsufuji, Y Murakami
1Department of Nutrition, Jikei University School of Medicine, Tokyo, Japan.
Abstract:
Since the catalytic-centre activity of mouse kidney ornithine decarboxylase (ODC) has been assumed to be twice as high as that of rat liver ODC, we compared relative catalytic-centre activity of the two enzymes by titration with antizyme, which inhibits ODC by stoichiometric binding. In either a crude or a purified state, both enzymes were inhibited by rat liver antizyme to the same extent, indicating that they have nearly identical catalytic-centre activities. This conclusion was supported by comparison of affinity labelling of the enzymes with alpha-difluoromethyl[14C]ornithine.
