Por favor, use este identificador para citar o enlazar este ítem: http://repositorio.ufc.br/handle/riufc/66604
Tipo: Artigo de Periódico
Título : Ultrastructural, physiological and biochemical analyses of chlorate toxicity on rice seedlings
Autor : Borges, Regis
Miguel, Emilio de Castro
Dias, Janice Maria Ribeiro
Cunha, Maura da
Smith, Ricardo Enrique Bressan
Oliveira, Jurandi Gonçalves de
Souza Filho, Gonçalo Apolinario de
Palabras clave : Chlorate stress;Chloroplast ultrastructure;Photochemical efficiency of PSII;Rice;Root anatomy
Fecha de publicación : 2004
Editorial : Plant Science
Citación : BORGES, Regis et al. Ultrastructural, physiological and biochemical analyses of chlorate toxicity on rice seedlings. Plant Science, [s.l.], v. 166, n. 4, p. 1057-1062, 2004.
Abstract: Chlorates are oxidizing substances considered phytotoxic to all green plant parts. In this study the physiological, biochemical and ultrastructural effects of chlorate treatments were studied in rice seedlings grown at two different temperatures (28 and 6 ◦C). Visual analyses demonstrated that the chlorate treatment provoked severe damage to plant leaves only at 28 ◦C. The electron microscopy of the chloroplast revealed several changes in the organelle organization, whose integrity of outer membrane and the internal network of thylakoid membranes were almost completely lost. A high level of lipid peroxidation was observed in 28 ◦C-chlorate-treated leaves in comparison to plants exposed to 6 ◦C-chlorate treatment. Photochemical efficiency of photosynthesis (Fv/Fm) was drastically affected by the 28 ◦C-chlorate treatment but, at low temperature, chlorate-treated plants suffered a discrete reduction in Fv/Fm. Root structure and organization were analyzed by light microscopy (LM) and scanning electron microscopy (SEM). The 28 ◦C-chlorate treatment provoked severe damages to the exodermis, ndodermis, cortex cells and root hairs. In the 6 ◦C-chlorate treatment, damage to root cells was also observed, but at a lower intensity. Nitrate reductase (NR) activity was analyzed and revealed the involvement of this enzyme in the chlorate action, even at a low temperature.
URI : http://www.repositorio.ufc.br/handle/riufc/66604
ISSN : 0168-9452
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