Abstract
Summary In the present work ornithine-, arginine- and S-adenosylmethionine decarboxylase activities were found in chloroplasts of Pinus radiata D. Don cotyledons and in isolated mitochondria from activated slices of Helianthus tuberosus L. tubers. Buffer molarity and pH optima were determined for each enzyme. In organelles different ratios between free polyamine contents were found with respect to the entire cell. Most of the S-adenosylmethionine decarboxylase activity was found in the 26,000 g supernatant of both plants where arginine and ornithine decarboxylase activities were markedly lower. Arginase activity was also detected in mitochondria. The different ratios between the enzyme activities in the various subcellular fractions of both systems may be an indication that these are effectively compartmentalized.
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