THE A12 ACETYLCHOLINESTERASE AND POLYPEPTIDE COMPOSITION OF ELECTRIC ORGAN BASAL LAMINA OF ELECTROPHORUS AND SOME TORPEDINAE FISHES

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dc.contributor.authorINESTROSA, NC
dc.contributor.authorMENDEZ, B
dc.date.accessioned2025-01-23T19:43:51Z
dc.date.available2025-01-23T19:43:51Z
dc.date.issued1983
dc.description.abstractBasal lamina (BL) of Torpedo, Discopyge and Electrophorus electric organs was purified in order to establish polypeptide composition and association with acetylcholinesterase (AChE). BL apparently presents a distinct peptide pattern and that the A12 form of AChE is directly attached to it. Comparison of the species studied demonstrated similarities both in polypeptide composition and AChE content of the purified BL. Extractions of BL with solutions of high ionic strength, guanidine-HCl and acetic acid indicated the differential solubilization of various domains of BL polypeptides.
dc.fuente.origenWOS
dc.identifier.eissn1099-0844
dc.identifier.issn0263-6484
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99846
dc.identifier.wosidWOS:A1983RR61600006
dc.issue.numero1
dc.language.isoen
dc.pagina.final48
dc.pagina.inicio41
dc.revistaCell biochemistry and function
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleTHE A12 ACETYLCHOLINESTERASE AND POLYPEPTIDE COMPOSITION OF ELECTRIC ORGAN BASAL LAMINA OF ELECTROPHORUS AND SOME TORPEDINAE FISHES
dc.typeartículo
dc.volumen1
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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