[Adenosine triphosphatases of cestodes Bothriocephalus scorpii].
Activities and properties of adenosine triphosphatases (ATPases) have been studied in mitochondrial and microsomal fractions of cestodes Bothriocephalus scorpii parasitizing in pyloric appendages of the Brandt's bullhead Myoxocephalus brandti. The highest activity has been revealed in the mitochondrial fraction. The mitochondrial and microsomal fractions of B. scorpii have the ATPase activity dependent on the presence of cations Mg2+, Mn2+, and Ca2+. Effects of ions and inhibitors on the B. scorpii ATPase activity with various cations have been studied. Both subcellular fractions are able to hydrolyze, apart from ATP, also GTP, CTP, and UTP.
Burenina
E A
EA
D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000818:Animals; D002413:Cations, Divalent; D002589:Cestoda / Q000201:enzymology*; D015801:Helminth Proteins / Q000737:chemistry*; D008670:Metals / Q000737:chemistry; D008928:Mitochondria / Q000201:enzymology*; D024101:Mitochondrial Proteins / Q000737:chemistry*; D012265:Ribonucleotides / Q000737:chemistry; D013379:Substrate Specificity
D002413:Cations, Divalent; D015801:Helminth Proteins; D008670:Metals; D024101:Mitochondrial Proteins; D012265:Ribonucleotides; D000251:Adenosine Triphosphatases