A MEMBRANE-ASSOCIATED DIMER OF ACETYLCHOLINESTERASE FROM XENOPUS SKELETAL-MUSCLE IS SOLUBILIZED BY PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE-C

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dc.contributor.authorINESTROSA, NC
dc.contributor.authorFUENTES, ME
dc.contributor.authorANGLISTER, L
dc.contributor.authorFUTERMAN, AH
dc.contributor.authorSILMAN, I
dc.date.accessioned2025-01-23T19:24:36Z
dc.date.available2025-01-23T19:24:36Z
dc.date.issued1988
dc.description.abstractThe susceptibility to phosphatidylinositol-specific phospholipase C of the membrane associated acetylcholinesterase (AChE) forms of Xenopus laevis skeletal muscle was examined. This treatment released almost all the detergent-soluble AChE species from muscle homogenates. Sucrose gradient analysis showed that the released acetylcholinesterase form corresponds to a hydrophilic G2 dimer, indicating that this dimer has a glycolipid anchoring domain which contains phosphatidylinositol.
dc.fuente.origenWOS
dc.identifier.eissn1872-7972
dc.identifier.issn0304-3940
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99377
dc.identifier.wosidWOS:A1988P228500034
dc.issue.numero1-2
dc.language.isoen
dc.pagina.final190
dc.pagina.inicio186
dc.revistaNeuroscience letters
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleA MEMBRANE-ASSOCIATED DIMER OF ACETYLCHOLINESTERASE FROM XENOPUS SKELETAL-MUSCLE IS SOLUBILIZED BY PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE-C
dc.typeartículo
dc.volumen90
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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