A. Pagliarani et al., MUSSEL MICROSOMAL NA-MG2+-ATPASE SENSITIVITY TO WATERBORNE MERCURY, ZINC AND AMMONIA(), Comparative biochemistry and physiology. Part C, Pharmacology toxicology & endocrinology, 113(2), 1996, pp. 185-191
1. In Mytilus galloprovincialis Lam. both the Na+ + K+)- and the Na+-A
TPases show a tissue- and dose dependent response to mercury (0.1 and
0.25 mg . L(-1) Hg2+), zinc (0.5 and 1.0 mg . L(-1) Zn2+) and ammonia
(0.4 and 1.0 mg . L(-1) ammonia-N). 2. The two ATPases were generally
more susceptive to the toxicants in the gills than in the mantle; in t
he case of heavy metals this finding complies with the higher metal in
corporation in the gills with respect to the mantle. 3. In the gills t
he two ATPase inhibition by mercury was enhanced by the co-presence of
environmental 0.4 mg . L(-1) ammonia-N; zinc removed the (Na+ + K+)-A
TPase inhibition by 0.1 mg . L(-1) Hg2+ as well as the enzyme activati
on promoted by 0.4 mg . L(-1) ammonia-N; both ATPases were inhibited b
y the 1.0 mg . L(-1) ammonia-N treatment. 4. Mantle ATPases were appar
ently refractory to mercury but not to zinc: the (Na+ + K+)-ATPase was
similarly stimulated by the exposure to 1.0 mg . L(-1) Zn2+ and to th
e mixture Zn2+ + Hg2+ and unaffected by 0.5 mg . L(-1) Zn2+ alone; the
Na+-ATPase was depressed by the exposures to 1.0 mg . L(-1) ammonia-N
and to the mixture Zn2+ + ammonia-N and conversely stimulated by Hg2 + ammonia-N, whereas all other treatments were uneffective. 5. In vit
ro approaches pointed out a susceptivity to the toxicants only for the
(Na+ + K+)-ATPase. The enzyme response in vitro often differed from t
hat in vivo.