BINDING OF THE ASYMMETRIC FORMS OF ACETYLCHOLINESTERASE TO HEPARIN

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dc.contributor.authorBRANDAN, E
dc.contributor.authorINESTROSA, NC
dc.date.accessioned2025-01-23T19:43:47Z
dc.date.available2025-01-23T19:43:47Z
dc.date.issued1984
dc.description.abstractThe interaction between acetylcholinesterase (EC 3.1.1.7) and heparin, a sulfated glycosaminoglycan, was studied by affinity chromatography. A specific binding of the asymmetric acetylcholinesterase to an agarose gel containing covalently bound heparin was demonstrated. This interaction required an intact collagenous tail, shown by the fact that the binding is abolished by pretreatment with collagenase. Globular forms did not bind to the column. Total and intracellular asymmetric acetylcholinesterase forms isolated from the endplate region of the rat diaphragm muscle showed higher affinity for the heparin than did the enzyme from the non-endplate region. Binding to the resin was destabilized with 0.55 M NaCl, and, among the various glycosaminoglycans tested, only heparin was able to displace the acetylcholinesterase bound to the column. Apparently, asymmetric acetylcholinesterase forms are immobilized on the synaptic basal lamina via interactions with heparin-like molecules, probably related to heparan sulfate proteoglycans.
dc.fuente.origenWOS
dc.identifier.eissn1470-8728
dc.identifier.issn0264-6021
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99818
dc.identifier.wosidWOS:A1984TB21000017
dc.issue.numero2
dc.language.isoen
dc.pagina.final422
dc.pagina.inicio415
dc.revistaBiochemical journal
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleBINDING OF THE ASYMMETRIC FORMS OF ACETYLCHOLINESTERASE TO HEPARIN
dc.typeartículo
dc.volumen221
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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