DIFFERENT MEMBRANE-BOUND FORMS OF ACETYLCHOLINESTERASE ARE PRESENT AT THE CELL-SURFACE OF HEPATOCYTES

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dc.contributor.authorPERELMAN, A
dc.contributor.authorBRANDAN, E
dc.date.accessioned2025-01-23T19:23:55Z
dc.date.available2025-01-23T19:23:55Z
dc.date.issued1989
dc.description.abstractIn the present study we have determinated the acetylcholinesterase molecular forms present in rat liver hepatocytes; we have also studied the association of acetylcholinesterase with the cell surface of the hepatocytes. Subcellular fractionation indicated that rough endoplasmic reticulum and plasma-membrane-enriched fractions contains G4 and G2 acetylcholinesterase forms bound to membranes. Hepatocytes incubated with phosphatidylinositol-specific phospholipase C released about 70% of the surface acetylcholinesterase. Sedimentation analysis showed that all the solubilized acetylcholinesterase activity comes exclusively from a G2 dimer. The G4 hydrophobic form of acetylcholinesterase accounts for the additional cell-surface activity. The existence of these two forms of acetylcholinesterase on the surface of hepatocytes was further established by analyzing the phosphatidylinositol-specific phospholipase C sensitivity of the acetylcholinesterase molecular forms present in isolated rat liver plasma membranes.
dc.fuente.origenWOS
dc.identifier.issn0014-2956
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99283
dc.identifier.wosidWOS:A1989AA13100026
dc.issue.numero1
dc.language.isoen
dc.pagina.final207
dc.pagina.inicio203
dc.revistaEuropean journal of biochemistry
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleDIFFERENT MEMBRANE-BOUND FORMS OF ACETYLCHOLINESTERASE ARE PRESENT AT THE CELL-SURFACE OF HEPATOCYTES
dc.typeartículo
dc.volumen182
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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