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Title: Purified omega-conotoxin GVIA receptor of rat brain resembles a dihydropyridine-sensitive L-type calcium channel

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (United States)
; ; ;  [1];  [2]
  1. Johns Hopkins Medical Inst., Baltimore, MD (United States)
  2. Univ. of California, Riverside (United States)

The {omega}-conotoxin GVIA (CTX) receptor has been purified 1,900-fold to apparent homogeneity by monitoring both reversible binding of {sup 125}I-labeled CTX ({sup 125}I-CTX) and photoincorporation of N-hydroxysuccinimidyl-4-azidobenzoate-{sup 125}I-CTX (HSA-{sup 125}I-CTX). Photoincorporation of HSA-{sup 125}I-CTX into a 230-kDa protein exhibits a pharmacologic and chromatographic profile indicating that the 230-kDa protein is the CTX-binding subunit of the receptor. The pharmacologic specificity of {sup 125}I-CTX binding to the purified CTX receptor closely resembles that of the native membrane-bound form with respect to sensitivity towards CTX and other peptide toxin antagonists. The purified CTX receptor comprises the 230-kDa protein ({alpha}{sub 1}) and four additional proteins with apparent molecular masses of 140 ({alpha}{sub 2}), 110, 70 ({beta}{sub 2}), and 60({beta}{sub 1}) kDa. This subunit structure closely resembles that of the 1,4-dihydropyridine-sensitive L-type calcium channel.

OSTI ID:
5823159
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 88:24; ISSN 0027-8424
Country of Publication:
United States
Language:
English