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Phospho hydrolase activity of the isolated brush border membrane of hymenolepis diminuta cestoda following sodium dodecyl sulfate poly acrylamide gel electrophoresis



Phospho hydrolase activity of the isolated brush border membrane of hymenolepis diminuta cestoda following sodium dodecyl sulfate poly acrylamide gel electrophoresis



Journal of Parasitology 66(6): 914-919



Following electrophoresis of isolated, brush-border membranes of H. diminuta on SDS[sodium dodecyl sulfate]polyacrylamide gels, 3 distinct areas of .alpha.-naphthyl phosphate (NP) hydrolysis were detected; these corresponded to proteins with MW of 106,800, 172,700 and > 340,000 daltons. Hydrolysis of NP was inhibited by ATP adenosine-5'-monophosphate, p-nitrophenylphosphate, glucose-1-phosphate, G-6-P, fructose-6-phosphate, fructose-1,6-diphosphate, molybdate, EDTA and ethyleneglycol-bis-(.beta.-amino-ethyl ether)-N,N'-tetraacetate (EGTA), but not by fluoride. Inhibition of NP hydrolysis by EDTA was relieved in the presence of Mg2+ or Ca2+. Heating the isolated, brush-border membrane in the presence of SDS for 5 min at 95.degree. C destroyed all enzymatic activity. These characteristics indicated that the enzyme( s) responsible for NP hydrolysis (following separation of membrane proteins by SDS-polyacrylamide gel electrophoresis) were the same enzymes responsible for the phosphohydrolase activity associated with intact and solubilized, brush-border membrane preparations of H. diminuta.

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Accession: 006104812

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Phosphohydrolase activity of the isolated, brush-border membrane of Hymenolepis diminuta (Cestoda) following sodium dodecyl sulfate (SDS) - polyacrylamide gel electrophoresis. Journal of Parasitology 666: 914-919, 1980

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