Abstract
1. 1. Partially purified rat liver ornithine decarboxylase is inhibited by several diamines including putrescine, 1,3-diaminopropane, cadaverine and p-phenylenediamine. 2. 2. The inhibition is dependent on pH, being strong at pH above 8 and negligible below pH 6.5. 3. 3. The kinetic study of the inhibition showed that while the aromatic diamine behaved as a simple competitive inhibitor, the aliphatic diamines presented a more complex pattern of inhibition in which two molecules of inhibitor might bind to the enzyme active site. 4. 4. The K I values for the different inhibitors were calculated and the degree of affinity for the enzyme was p-phenylenediamine > putrescine > cadaverine > 1,3-diaminopropane. 5. 5. A molecular mechanism explaining how one or two molecules of inhibitor can bind to the enzyme is proposed.
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