The nicotinic acetylcholine receptors (nAChR) in skeletal muscle, which are targets of the autoimmune response that cause myasthenia gravis (MG). MG is an autoimmune disease caused by anti-acetylcholine (anti-AChR) antibodies, resulting in functional loss of AChR at the neuromuscular junction. Specific binding of radio-iodinated α and β Bgtx was carried out in membranes (rapid filtration method) and triton extract (ammonium sulfate precipitation method) of fresh muscle. The specific binding of α Bgtx to membranes and triton extract of fresh muscle was found to be 19.8 ± 0.2 and 10.2 ± 0.12 fmoles/mg tissue, respectively whereas the same for β-Bgtx was found to be 10.2 ± 0.15 and 7.2 ± 0.12 fmoles/mg tissue, respectively. It was observed that there was no significant decline in specific binding to membranes and triton extract of muscle with increase in post-mortem time from 5 to 24 h. By indirect ELISA with MG pool sera, in addition to age the immunoreactivity varies from one cadaver to another. It was observed that β bungarotoxin binding proteins in muscle shows high immunoreactivity as compared to α Bungarotoxin binding protein.