Abstract
An NADP-dependent isocitrate dehydrogenase (NADP-IDH) activity was measured in a Percoll purified mitochondrial fraction from axes of germinating sunflower ( Helianthus annuus, L.) seeds. Fraction enrichment in mitochondria was revealed by marker enzyme activities and by electron microscopy which showed no contamination by other organelles and indicated that no fragmentation of mitochondria had occurred during their preparation. More than 95% of the NADP-IDH activity was latent; it was found to be different from the mitochondrial NAD-IDH activity by competition assay. Mitochondrial NADP-IDH was electrophoretically and immunologically different from the NAD-specific and the cytosolic NADP-specific isoforms. The enzyme activity from mitochondrial matrix extract was eluted from Superose 12 with a molecular weight of 70 kDa. A possible physiological role of the mitochondrial NADP-IDH is discussed.
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