The A12 acetylcholinesterase and polypeptide composition of electric organ basal lamina of electrophorus and some torpedinae fishes

Nibaldo C. Inestrosa, Bernardita Méndez

Resultado de la investigación: Article

11 Citas (Scopus)

Resumen

Basal lamina (BL) of Torpedo, Discopyge and Electrophorus electric organs was purified in order to establish polypeptide composition and association with acetylcholinesterase (AChE). Results indicate that BL 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.

Idioma originalEnglish
Páginas (desde-hasta)41-48
Número de páginas8
PublicaciónCell Biochemistry and Function
Volumen1
N.º1
DOI
EstadoPublished - 1983

Huella dactilar

Electrophorus
Electric Organ
compound A 12
Acetylcholinesterase
Basement Membrane
Fish
Fishes
Peptides
Chemical analysis
Torpedo
Ionic strength
Acetic Acid
Osmolar Concentration
Association reactions

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Cell Biology
  • Medicine(all)

Citar esto

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abstract = "Basal lamina (BL) of Torpedo, Discopyge and Electrophorus electric organs was purified in order to establish polypeptide composition and association with acetylcholinesterase (AChE). Results indicate that BL 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.",
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The A12 acetylcholinesterase and polypeptide composition of electric organ basal lamina of electrophorus and some torpedinae fishes. / Inestrosa, Nibaldo C.; Méndez, Bernardita.

En: Cell Biochemistry and Function, Vol. 1, N.º 1, 1983, p. 41-48.

Resultado de la investigación: Article

TY - JOUR

T1 - The A12 acetylcholinesterase and polypeptide composition of electric organ basal lamina of electrophorus and some torpedinae fishes

AU - Inestrosa, Nibaldo C.

AU - Méndez, Bernardita

PY - 1983

Y1 - 1983

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AB - Basal lamina (BL) of Torpedo, Discopyge and Electrophorus electric organs was purified in order to establish polypeptide composition and association with acetylcholinesterase (AChE). Results indicate that BL 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.

KW - AChR clusters

KW - basal lamina peptides

KW - cholinergic synapse

KW - electric organ

KW - extracellular matrix

KW - Polypeptides

KW - synaptic AChE A form

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JO - Cell Biochemistry and Function

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