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

✍ Scribed by Peter W. Pappas


Book ID
115899713
Publisher
Elsevier Science
Year
1981
Tongue
English
Weight
925 KB
Volume
51
Category
Article
ISSN
0014-4894

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Acid phosphatase activity in the isolate
✍ Peter W. Pappas 📂 Article 📅 1988 🏛 John Wiley and Sons 🌐 English ⚖ 497 KB

The isolated brush border membrane of the tapeworm, Hymenolepis diminuta, hydrolyzes p-nitrophenyl phosphate over a broad pH range. Acid phosphatase activity (pH optimum at 4.0) is inhibited specifically by sodium dodecyl sulfate (SDS) and NaF, while the alkaline phosphatase activity (pH optimum at

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✍ Peter W. Pappas; David A. Leiby 📂 Article 📅 1989 🏛 John Wiley and Sons 🌐 English ⚖ 528 KB

Several compounds were tested as inhibitors of the alkaline phosphatase (AlkPase) activity associated with the isolated brush border membrane of the tapeworm, Hymenolepis diminuta. Molybdate, arsenate, arsenite and P-glycerophosphate (BGP) were competitive inhibitors of the hydrolysis of pnitropheny