Summary
The activity of pyruvate decarboxylase, PDC (EC 4.1.1.17), in the primary roots of maize seedlings exposed to anoxic conditions was examined: such treatment resulted in a time-dependent increase of enzymatic activity. We identified the polypeptide associated with PDC activity by two dimensional gel electrophoresis of electrophoretic mobility variants. The incorporation of radioactive amino acids into this polypeptide under anoxic conditions indicated that the increase in enzymatic activity was accompanied by the de novo synthesis of the PDC polypeptide and therefore identified PDC as one of the anaerobic proteins of maize. The increase in PDC activity paralleled that of alcohol dehydrogenase, ADH. Since PDC and ADH catalyze sequential reactions of the Embden-Meyerhoff pathway, our results define a system of apparent coordinate regulation of the expression of two metabolically related enzymatic activities in maize.
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Laszlo, A., St. Lawrence, P. Parallel induction and synthesis of PDC and ADH in anoxic maize roots. Molec Gen Genet 192, 110–117 (1983). https://doi.org/10.1007/BF00327655
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DOI: https://doi.org/10.1007/BF00327655