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The A 12 acetylcholinesterase and polypeptide composition of electric organ basal lamina of electrophorus and some torpedinae fishes
Author(s) -
Inestrosa Nibaldo C.,
Méndez Bernardita
Publication year - 1983
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.290010108
Subject(s) - basal lamina , acetylcholinesterase , basal (medicine) , composition (language) , biology , electric organ , anatomy , zoology , biochemistry , endocrinology , enzyme , ultrastructure , receptor , art , torpedo , acetylcholine receptor , literature , insulin
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 A 12 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.