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- W2068609524 abstract "A partially purified inorganic pyrophosphatase from Ascaridia galli, a nematode parasite of chickens has been investigated. The enzyme was activated by Mg++ and Zn++ and to a lesser extent by Co++, Mn++, Fe++, Cu++, and Ca++. In combination with Mg++ the other divalent ions were inhibitory. Cadmium and fluoride, both effective anthelmintics, inhibited markedly at low concentrations. Piperazine adipate, another anthelmintic, did not inhibit the enzyme. Tetracycline, oxytetracycline, chloromycetin, EDTA and ATP all inhibited the PPase. Optimum pH with Mg++ as activator was 6.8 to 7.2 but with Zn++ 6.2 to 6.5 was the optimum range. A Michaelis constant (Km) was estimated by the conventional Lineweaver-Burk treatment. Km was 6.4 × 10−4M, in fair agreement with Km values of PPases from other sources." @default.
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- W2068609524 date "1959-06-01" @default.
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- W2068609524 title "Studies in helminth enzymology. II. Properties of an inorganic pyrophosphatase from Ascaridia galli, a nematode parasite of chickens" @default.
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- W2068609524 doi "https://doi.org/10.1016/0014-4894(59)90026-8" @default.
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