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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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
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