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Papel de las actividades superóxido dismutasa y catalasa en la ...

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RESULTS AND DISCUSSION<br />

resist 100 mM of peroxi<strong>de</strong>, a lethal conc<strong>en</strong>tration without peroxi<strong>de</strong> pretreatm<strong>en</strong>t. In the<br />

case of P. damse<strong>la</strong>e subsp. piscicida, it is interesting to note that a significant increase<br />

in survival rates of the non-virul<strong>en</strong>t strain was observed wh<strong>en</strong> cultures were pulsed with<br />

hydrog<strong>en</strong> peroxi<strong>de</strong> compared to cells cultured until stationary phase. In contrast, this<br />

increase has not be<strong>en</strong> observed for the virul<strong>en</strong>t strain, which always showed higher<br />

survival regardless of the growth phase, or the pulse with hydrog<strong>en</strong> peroxi<strong>de</strong>.<br />

On the other hand, culture un<strong>de</strong>r iron-restricted conditions results in a significant<br />

<strong>de</strong>crease in survival of both virul<strong>en</strong>t and avirul<strong>en</strong>t strains. The fact that this bacterial<br />

species contains a ferric cata<strong><strong>la</strong>s</strong>e (article 1.2., Article section), whose activity is reduced<br />

un<strong>de</strong>r iron limiting conditions, may exp<strong>la</strong>in this result.<br />

Superoxi<strong>de</strong> dismutase and cata<strong><strong>la</strong>s</strong>e are metallo<strong>en</strong>zymes that can possess differ<strong>en</strong>t<br />

metals in their active c<strong>en</strong>tre. Microorganisms capable to produce differ<strong>en</strong>t superoxi<strong>de</strong><br />

dismutase and cata<strong><strong>la</strong>s</strong>e iso<strong>en</strong>zymes, <strong>de</strong>p<strong>en</strong>ding on culture conditions, have be<strong>en</strong><br />

<strong>de</strong>scribed. These culture conditions inclu<strong>de</strong> oxyg<strong>en</strong> levels, low iron levels or growth<br />

until stationary phase (Storz et al., 1990; Privalle and Fridovich, 1992; Crockford et al.,<br />

1995; Schnell and Steinman, 1995; Barnes et al., 1996; Po<strong>la</strong>ck et al., 1996; St. John and<br />

Steinman, 1996; Lynch and Kuramitsu, 2000; Yesilkaya et al., 2000; Geslin et al., 2001;<br />

Vattanaviboon and Mongkolsuk, 2001).<br />

Results obtained in the pres<strong>en</strong>t work show that P. damse<strong>la</strong>e subsp. piscicida does<br />

not synthetize a new form of superoxi<strong>de</strong> dismutase or cata<strong><strong>la</strong>s</strong>e wh<strong>en</strong> cultured un<strong>de</strong>r<br />

assayed conditions. Thus, all strains show only one band of superoxi<strong>de</strong> dismutase<br />

activity, with simi<strong>la</strong>r electrophoretic mobility to ferric superoxi<strong>de</strong> dismutase <strong>de</strong>scribed<br />

by Barnes et al. (1999a). Ev<strong>en</strong> oxidative stress, by hydrog<strong>en</strong> peroxi<strong>de</strong> or paraquat (an<br />

oxyg<strong>en</strong>ic radical g<strong>en</strong>erator) addition, did not induce the synthesis of a differ<strong>en</strong>t<br />

iso<strong>en</strong>zyme, unlike CuZnSOD and MnSOD <strong>de</strong>scribed in Escherichia coli (Hassan and<br />

Fridovich, 1977; Privalle and Fridovich, 1992; B<strong>en</strong>ov and Fridovich, 1994; Geslin et al.,<br />

2001), MnSOD in A. salmonicida (Barnes et al., 1996; Barnes et al., 1999b),<br />

Pseudomonas aeruginosa (Po<strong>la</strong>ck et al., 1996) and Streptococcus pneumoniae<br />

(Yesilkaya et al., 2000). Neither restrictive iron conditions induce MnSOD synthesis<br />

(Privalle and Fridovich, 1992; Barnes et al., 1999b). Although further studies would be<br />

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