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Hymenolepis diminuta: Partial characterization of the membrane-bound and solubilized alkaline phosphohydrolase activities of the isolated brush border plasma membrane

โœ Scribed by Peter W. Pappas

Book ID
115899778
Publisher
Elsevier Science
Year
1982
Tongue
English
Weight
558 KB
Volume
54
Category
Article
ISSN
0014-4894

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๐Ÿ“œ SIMILAR VOLUMES

Acid phosphatase activity in the isolate
Acid phosphatase activity in the isolated brush border membrane of the tapeworm, Hymenolepis diminuta: Partial, characterization and differentiation from the alkaline phosphatase activity
โœ Peter W. Pappas ๐Ÿ“‚ Article ๐Ÿ“… 1988 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 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

Competitive, uncompetitive, and mixed in
Competitive, uncompetitive, and mixed inhibitors of the alkaline phosphatase activity associated with the isolated brush border membrane of the tapeworm Hymenolepis diminuta
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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