Abstract
Although decarboxylases, particularly ornithine decarboxylase, are of considerable importance in cell metabolism, it has been impossible to demonstrate their activity histochemically, as this depends on trapping carbon dioxide at neutral pH values. A new reagent, lead hydroxyisobutyrate, has been shown capable of such trapping. It has been applied to the demonstration of ornithine decarboxylase activity in mouse kidney. Optimal concentrations of substrate, co-factor and trapping agent, as well as the pH optimum, have been determined for cryostat sections stabilized with a collagen polypeptide. The activity was inhibited by the specific ornithine decarboxylase inhibitor alpha-difluoromethyl ornithine.
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