Abstract
Ornithine decarboxylase activity in extracts of phytohaemagglutinin-stimulated human lymphocytes is rapidly and extensively inhibited by additions of micromolar concentrations of putrescine or spermidine to the culture medium. This inhibition is not due to feedback inhibition of the enzyme by putrescine, spermidine or their metabolites. Inhibition is dependent on the continuation of protein synthesis, but does not require RNA synthesis. The effect of putrescine is abolished when its conversion into spermidine by the cells is prevented.
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