In extracts from the youngest leaves ofArena sativa, Hordeam vulgare, Zea Mays, Pisum sativum, Phaseolus vulgaris, Lactuca sativa, and four pyrrolizidine alkaloid-bearing species of Heliotropium, the activities of ornithine decarboxylase, close to V.n, ranged between traces and 1.5 nanomoles per hour per gram fresh weight when based on putrescine formed during incubation with labeled orDithine. The arginine decarboxylase activities in the same extracts ranged between 8 and 8000 nanomoles per hour per gram fresh weight being lowest in the borages and highest in oat and barley. a-Difluoromethylornithine and a-difluoromethyharginine inhibited ornithine and arginine decarboxylases, respectively, in all species. Agmatine, putrescine, spermidine, and spermine were found in all, diaminopropane in eight, and cadaverine in three species.No correlation was observed between arginine or ornithine decarboxylase level and the levels of total polyamines. The in vitro decarboxylase activities found in the borages cannot explain the high accumulation of putrescine-derived pyrrolizidines in their youngest leaves if the pyrrolizidines are produced in situ from arginine and/or ornithine as precursors; other possibilities are discussed.In assays of ornithine decarboxylase, an interference of decarboxylation not due to this enzyme was observed in extracts from all species. In arginine decarboxylase assays, the interfering decarboxylation as well as the interference of arginase were apparent in two species. Addition of aminoguanidine was needed to suppress oxidative degradation of putrescine and agmatine during incubation of extracts from pea, bean, lettuce, Heliotropium angiospermum, and Heliotropium indicum.When assayed for ADC2 and/or ODC using [1l-'4C]-or [U-'4C]-labeled Arg and/or Orn, respectively, leaf extracts from oat, tomato, and especially form Heliotropium angiospermum exhibited significant decarboxylation of the substrates that was not due to activities of the assayed enzymes (6). Additional artifacts such as oxidative degradation of Agm and Put as well as conversion of Arg into Orn were observed in extracts from H. angiospermum, especially in Tris-HC buffer. However, addition of AG, the amine oxidase inhibitor, at 0.1 to 0.2 mM and of Orn, the competitive inhibitor of arginase, at 20 mm permitted estimation ofADC and ODC activities on the basis ofAgm and Put ' This work was performed during a sabbatical (H. B.) at Merrell Dow Research Institute, Cincinnati, OH.