AMPHIPHILIC BEHAVIOR OF A BRAIN TETRAMERIC ACETYLCHOLINESTERASE FORM LACKING THE PLASMA-MEMBRANE ANCHORING DOMAIN

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dc.contributor.authorFUENTES, ME
dc.contributor.authorINESTROSA, NC
dc.date.accessioned2025-01-23T19:22:08Z
dc.date.available2025-01-23T19:22:08Z
dc.date.issued1992
dc.description.abstractWe have studied the behavior of a mammalian brain tetrameric acetylcholinesterase (AChE) form released by proteinase K from a crude membrane fraction of bovine caudate nucleus. The solubilization of active AChE indicated the presence of a protease-sensitive site in the anchored protein. Unexpectedly, the solubilized AChE maintained its capacity to form aggregates in detergent-free gradients. We demonstrate here that this property was due neither to the presence of the hydrophobic membrane-anchoring domain still linked to the enzyme, nor to the presence of AChE activity trapped in small plasma membrane vesicles. Moreover, we found that the proteinase K-treated extract, devoid of AChE activity, induced the aggregation of purified hydrophilic AChE which usually does not form aggregates. Our results suggest the presence of an AChE aggregating factor in bovine brain extracts prepared in the presence of proteinase K. It is possible that this aggregation may reflect a process of AChE clustering on neurons.
dc.fuente.origenWOS
dc.identifier.issn0006-8993
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/98973
dc.identifier.wosidWOS:A1992HZ74700001
dc.issue.numero1-2
dc.language.isoen
dc.pagina.final5
dc.pagina.inicio1
dc.revistaBrain research
dc.rightsacceso restringido
dc.subjectBRAIN TETRAMERIC ACETYLCHOLINESTERASE
dc.subjectAGGREGATING FACTOR
dc.subjectHYDROPHILIC FORM
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleAMPHIPHILIC BEHAVIOR OF A BRAIN TETRAMERIC ACETYLCHOLINESTERASE FORM LACKING THE PLASMA-MEMBRANE ANCHORING DOMAIN
dc.typeartículo
dc.volumen580
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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