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The omega-conotoxin GVIA (CTX) receptor has been purified 1900-fold to apparent homogeneity by monitoring both reversible binding of 125I-labeled CTX (125I-CTX) and photoincorporation of N-hydroxysuccinimidyl-4-azidobenzoate-125I-CTX (HSA-125I-CTX). Photoincorporation of HSA-125I-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 125I-CTX binding to the purified CTX receptor closely resembles that of the native membrane-bound form with respect to sensitivity towards CTX (Kd = 32 pM) and other peptide toxin antagonists. The purified CTX receptor comprises the 230-kDa protein (alpha 1) and four additional proteins with apparent molecular masses of 140 (alpha 2), 110, 70 (beta 2), and 60 (beta 1) kDa. This subunit structure closely resembles that of the 1,4-dihydropyridine-sensitive L-type calcium channel.
M W McEnery, and
A M Snowman, and
A H Sharp, and
M E Adams, and
S H Snyder
November 1986,
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M W McEnery, and
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M W McEnery, and
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Protein science : a publication of the Protein Society,
M W McEnery, and
A M Snowman, and
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September 1996,
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M W McEnery, and
A M Snowman, and
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M W McEnery, and
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M E Adams, and
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January 1989,
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M W McEnery, and
A M Snowman, and
A H Sharp, and
M E Adams, and
S H Snyder
October 1987,
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M W McEnery, and
A M Snowman, and
A H Sharp, and
M E Adams, and
S H Snyder
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M W McEnery, and
A M Snowman, and
A H Sharp, and
M E Adams, and
S H Snyder
November 1993,
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M W McEnery, and
A M Snowman, and
A H Sharp, and
M E Adams, and
S H Snyder
July 1996,
Biochemistry,
