Specific Binding of Perhydrohistrionicotoxin to Torpedo Acetylcholine Receptor

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1979 Jun 1

PMID 288047

Citations 20

Authors

J Elliott

S M Dunn

S G Blanchard

M A RAFTERY

Affiliations

Soon will be listed here.

Abstract

Torpedo californica postsynaptic membrane fragments were treated with base, which resulted in membranes that were depleted of many nonacetylcholine receptor polypeptides and contained acetylcholine receptor subunits of Mr 40,000, 50,000, 60,000, and 65,000 (Raftery, M.A., Vandlen, R.L., Reed, K.L. & Lee T. (1975) Cold Spring Harbor Symp. Quant. Biol. 40, 193-202). A 43,000-Mr polypeptide and some other components were quantitatively extracted. Base-treated membranes retained the capacity to bind [3H]perhydrohistrionicotoxin and the local anesthetics dibucaine and tetracaine. The regulation of this binding by carbamylcholine, as well as the kinetic mechanism of perhydrohistrionicotoxin binding, was unchanged. [3H]Perhydrohistrionicotoxin binding activity was largely reconstituted from 2% sodium cholate extracts of base-treated membranes. Therefore, the perhydrostrionicotoxin binding site appears to be located on one or more of the acetylcholine receptor polypeptides, and the reconstitution of that binding site from detergent extracts does not require the presence of a 43,000-Mr polypeptide.

Citing Articles

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Photoaffinity labeling of Torpedo acetylcholine receptor at multiple sites.

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Residues 377-389 from the delta subunit of Torpedo californica acetylcholine receptor are located in the cytoplasmic surface.

Iriarte A, Martinez-Carrion M J Protein Chem. 1994; 13(1):67-76.

PMID: 8011073 DOI: 10.1007/BF01891994.

Thermal stability of Torpedo californica acetylcholine receptor in a cholesterol lipid environment.

Mol Cell Biochem. 1994; 132(2):91-9.

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Residues within the alpha subunit sequence 304-322 of muscle acetylcholine receptor forming autoimmune CD4+ epitopes in BALB/c mice.

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