Acetylcholinesterase in Schistosoma mansoni is anchored to the membrane via covalently attached phosphatidylinositol.
Mol Biochem Parasitol
; 29(2-3): 171-9, 1988 Jun.
Article
en En
| MEDLINE
| ID: mdl-3137466
Two enzymes, alkaline phosphatase and acetylcholinesterase (AChE), have been shown previously to be components of the surface of the trematode parasite Schistosoma mansoni. In this study we report that both these enzymes and other serine hydrolases are susceptible to release from the S. mansoni tegumental membrane by a phosphatidylinositol-specific phospholipase C (PIPLC) of bacterial origin. These data suggest that AChE and alkaline phosphatase of S. mansoni, as in higher organisms, are anchored to the membrane via covalently attached phosphatidylinositol. The release of AChE from the vesicular fraction of the parasite with PIPLC occurs in a concentration-dependent manner. Sucrose gradient centrifugation of the PIPLC-released AChE showed a single 8.3 S molecular form, similar to that observed for AChE solubilized by Triton X-100. PIPLC removed large amounts of AChE from the surface of intact schistosomula in culture, with no impairment of the viability of the parasite. In this case, an increase in the overall levels of AChE in the intact parasite was observed after addition of PIPLC.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fosfatidilinositoles
/
Fosfolipasas de Tipo C
/
Acetilcolinesterasa
/
Schistosoma mansoni
/
Proteínas de la Membrana
Límite:
Animals
Idioma:
En
Revista:
Mol Biochem Parasitol
Año:
1988
Tipo del documento:
Article
País de afiliación:
Israel
Pais de publicación:
Países Bajos