HEPARIN-ACETYLCHOLINESTERASE INTERACTION - SPECIFIC DETACHMENT OF CLASS I-A FORMS AND BINDING OF CLASS I AND CLASS-II-A FORMS TO HEPARIN-AGAROSE

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dc.contributor.authorBRANDAN, E
dc.contributor.authorLLONA, I
dc.contributor.authorINESTROSA, NC
dc.date.accessioned2025-01-23T19:26:41Z
dc.date.available2025-01-23T19:26:41Z
dc.date.issued1986
dc.description.abstractThis study describes the specificity, time-course and characteristics of the solubilization of class I-A forms of AChE by heparin, from the endplate regions of rat diaphragm muscle. Heparin fractions which differed in charge size, anticoagulant activity and capacity to bind type I collagen, were probed in their ability to extract AChE. No differences were found among all the fractions tested. Affinity chromatography on heparin-agarose of class I- and class II-A forms of esterase showed that both classes were able to bind to the column with the same relative affinity. Our results establish the use of heparin, as a solubilizing agent for the class I-A. The existence of a heparin-binding domain in class I- and class II-A forms of AChE, opens the possibility, that heparan sulfate proteoglycans could be involved in the anchorage of both types of esterase to synaptic regions. Finally, our results suggest that class I and class II-A do not correspond to intrinsically distinct molecules, but rather to identical molecules engaged in different interactions in the tissue.
dc.fuente.origenWOS
dc.identifier.eissn1872-9754
dc.identifier.issn0197-0186
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99642
dc.identifier.wosidWOS:A1986D854800010
dc.issue.numero1
dc.language.isoen
dc.pagina.final84
dc.pagina.inicio75
dc.revistaNeurochemistry international
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleHEPARIN-ACETYLCHOLINESTERASE INTERACTION - SPECIFIC DETACHMENT OF CLASS I-A FORMS AND BINDING OF CLASS I AND CLASS-II-A FORMS TO HEPARIN-AGAROSE
dc.typeartículo
dc.volumen9
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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