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Hymenolepis diminuta: partial characterization of membrane-bound nucleotidase-activities (ATPase and 5'-nucleotidase) in the isolated brush border membrane



Hymenolepis diminuta: partial characterization of membrane-bound nucleotidase-activities (ATPase and 5'-nucleotidase) in the isolated brush border membrane



Experimental Parasitology 51(2): 209-219



The pH optimum for ATPase in the isolated brush border membrane of Hymenolepis diminuta was 7.4 and divalent cations were required for maximum activity; no Na+ - K+ activated ATPase was present. ATPase activity was inhibited by molybdate and phosphorylated monosaccharides, but not by N-ethylmaleimide (NEM), p-chloromercuribenzoate (pCMB), or fluoride. The pH optimum for 5'-nucleotidase activity was 9.6 to 10.2 and divalent cations were necessary for maximum activity. 5'-Nucleotidase activity was inhibited by molybdate at pH 9.6 and 7.4, and activated by NEM and pCMB at pH 9.6 and 7.4, respectively; fluoride had no effect. Solubilization of the brush border membrane fraction in 1% sodium dodecyl sulphate had no inhibitory action on either enzyme activity.

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Accession: 000904346

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PMID: 6258963


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