A COMPARISON OF THE XENOPUS-LAEVIS OOCYTE ACETYLCHOLINESTERASE WITH THE MUSCLE AND BRAIN ENZYME SUGGESTS VARIATIONS AT THE POSTTRANSLATIONAL LEVEL
dc.contributor.author | MOYA, MA | |
dc.contributor.author | FUENTES, ME | |
dc.contributor.author | INESTROSA, NC | |
dc.date.accessioned | 2025-01-23T19:22:52Z | |
dc.date.available | 2025-01-23T19:22:52Z | |
dc.date.issued | 1991 | |
dc.description.abstract | 1. Xenopus laevis oocytes express endogenously two components of the cholinergic system: the muscarinic receptors and the acetylcholinesterase (AChE). | |
dc.description.abstract | 2. A biochemical characterization of this enzyme was carried out. | |
dc.description.abstract | 3. The results established that the activity found in the oocytes correspond to 'true' AChE with a molecular weight of 65,000 Da and a sedimentation coefficient of 3-4 S. | |
dc.description.abstract | 4. The enzyme aggregates in the absence of detergent suggesting that it possess an hydrophobic character; despite that, it is not sensitive to PIPLC. | |
dc.description.abstract | 5. A comparison with the Xenopus brain and muscle AChE shows different post-translational modifications and catalytic properties with the oocyte AChE. | |
dc.fuente.origen | WOS | |
dc.identifier.eissn | 1878-1659 | |
dc.identifier.issn | 1532-0456 | |
dc.identifier.uri | https://repositorio.uc.cl/handle/11534/99120 | |
dc.identifier.wosid | WOS:A1991FC28400007 | |
dc.issue.numero | 2-3 | |
dc.language.iso | en | |
dc.pagina.final | 305 | |
dc.pagina.inicio | 299 | |
dc.revista | Comparative biochemistry and physiology c-toxicology & pharmacology | |
dc.rights | acceso restringido | |
dc.subject.ods | 03 Good Health and Well-being | |
dc.subject.odspa | 03 Salud y bienestar | |
dc.title | A COMPARISON OF THE XENOPUS-LAEVIS OOCYTE ACETYLCHOLINESTERASE WITH THE MUSCLE AND BRAIN ENZYME SUGGESTS VARIATIONS AT THE POSTTRANSLATIONAL LEVEL | |
dc.type | artículo | |
dc.volumen | 98 | |
sipa.index | WOS | |
sipa.trazabilidad | WOS;2025-01-12 |