Three possible disulfides in the acetylcholine receptor α-subunit

R. Mosckovitz, J. M. Gershoni

Research output: Contribution to journalArticlepeer-review

Abstract

The cysteinyl residues of the acetylcholine receptor α-subunit of Torpedo californica were analyzed. All seven cysteines could be accounted for. Three possible disulfide bridges and one unpaired cysteine were indicated. The disulfide linkages were as follows: Cys128 to Cys142; Cys192 to Cys193; Cys412 to Cys418 (Cys222 is unpaired). The identification of cysteinyl residues was accomplished by a modified protein blot procedure. Cysteinyl residues of intact nicotinic acetylcholine receptor were selectively biotinylated with 3-(N-maleimidopropionyl)biocytin and subsequently detected by the 125I-labeled avidin overlay of blotted Staphylococcus aureus V8 proteolyzed α-subunits. Two pairs of cysteines (Cys128/Cys142 and Cys412/Cys418) could be demonstrated only after Na(BH4) reduction of the acetylcholine receptor. Cysteine residues 192 and 193 are particularly sensitive to reduction; 0.1 mM dithiothreitol is sufficient.

Original languageEnglish
Pages (from-to)1017-1022
Number of pages6
JournalJournal of Biological Chemistry
Volume263
Issue number2
StatePublished - 1988
Externally publishedYes

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