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Echinobase
ECB-ART-36373
Biometals 1996 Jul 01;93:277-83. doi: 10.1007/bf00817928.
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Impact of aluminium, fluoride and fluoroaluminate complex on ATPase activity of Nostoc linckia and Chlorella vulgaris.

Husaini Y , Rai LC , Mallick N .


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This study demonstrates a pH-dependent inhibition of Mg(2+)- and Ca(2+)-ATPase activities of Nostoc linckia and Chlorella vulgaris exposed to AlCl3, AlF3, NaF and AlCl3+NaF together. AlF3 and the combination of AlCl3+NaF were more inhibitory to both the enzymes as compared with AlCl3 and NaF. Toxicity of the test compounds increased with increasing acidity. Interaction of AlCl3+NaF was additive on N. linckia and C. vulgaris, respectively, at pH 7.5 and 6.8, and synergistic at pH 6.0 and 4.5. In the presence of 60 and 100 microM PO4(3-) an increased NaF concentration (in the AlCl3+NaF combination) was required to produce the same degree of inhibition in ATP synthesis and ATPase activity. Toxicity of fluoroaluminate was reduced in the presence of EDTA and citrate. Except for beryllium to some extent, combinations of cadmium, cobalt, iron, manganese, tin and zinc with fluoride were not as effective as aluminium in inhibiting the ATPase activity. The presence of a 100 kDa protein band in SDS-PAGE of both control as well as AlCl3+NaF-treated samples suggested that AlF4- inhibits the ATPase activity by acting as a functional barrier without affecting the structure of the enzyme.

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Genes referenced: impact LOC581395 LOC594261

References [+] :
Bigay, Fluoride complexes of aluminium or beryllium act on G-proteins as reversibly bound analogues of the gamma phosphate of GTP. 1987, Pubmed