An immunochemical approach to the identification of the MBTA binding site of the nicotinic acetylcholine receptor of Torpedo californica.
Monospecific anti-[4-(N-maleimidobenzyl) trimethylammonium] (MBTA) antibodies were prepared from sera of rabbits immunized with an albumin-MBTA conjugate and used to synthesize an MBTA-specific immunosorbent. Torpedo californica acetylcholine receptor was affinity labeled with [3H]-MBTA and proteolyzed extensively with pronase, and the peptide fraction of the digest chromatographed on the anti-MBTA resin. The amino acid composition of the purified MBTA-peptide fraction was compared with the sequences flanking the seven cysteinyl residues of the alpha-subunit. The best fit was observed with the segment containing cysteine 142.
D000345:Affinity Labels / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004557:Electric Organ / Q000378:metabolism*; D007106:Immune Sera; D046911:Macromolecular Substances; D000644:Quaternary Ammonium Compounds / Q000378:metabolism*; D011978:Receptors, Nicotinic / Q000302:isolation & purification / Q000378:metabolism*; D014101:Torpedo
D000345:Affinity Labels; D000596:Amino Acids; D007106:Immune Sera; D046911:Macromolecular Substances; D000644:Quaternary Ammonium Compounds; D011978:Receptors, Nicotinic; C008313:4-(N-maleimido)benzyltrimethylammonium