INV SUPERIOR JUBILADO
CASCONE Osvaldo
artículos
Título:
The nicotinic acetylcholine receptor from Discopyge Tschudii: purification, characterization and reconstitution into liposomes
Autor/es:
E.L.M. OCHOA; M.J. BISCOGLIO DE JIMÉNEZ BONINO; O. CASCONE; S. MEDRANO; M.B. COUSSEAU
Revista:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. PART B, BIOCHEMISTRY & MOLECULAR BIOLOGY.
Editorial:
ELSEVIER SCIENCE INC
Referencias:
Año: 1983 vol. 76 C p. 313 - 317
ISSN:
1096-4959
Resumen:
The nicotinic acetylcholine receptor from Discopyge tschudii electroplax was purified by affinity chromatography on Affi-Gel 401 using bromoacetylcholine as the ligand. Its specific activity was about 4000 pmol I125-bungarotoxin mg protein. SDS-polyacrilamide gel electrophoresis revealed four bands of apparent molecular weights: 41200, 49500, 60000 and 66300. The amino acid composition of each individual subunit was determined. Native membranes, rich in nicotinic receptor exhibited carbamylcholine-catalysed cation transport(blocked by curare and desensitized by prior incubation with the cholinergic agonist). The functional activity of the purified material could be reconstituted into soybean lecithin liposomes. Our data show that the Discopyge tschudii nicotinic receptor is similar to that from Torpedo californica.
