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High affinity β-bungarotoxin binding protein was purified from skeletal muscle of human cadaver by affinity chromatography using β-bungarotoxin as a ligand. The SDS-PAGE of purified protein revealed two major protein bands with molecular weight of 86 and 68 kD. The purified protein has a kD of 2.3±0.15 nmoles and binding sites of 34±2.3 f mole/mg tissue. Immunoreactivity profile of purified presynaptic receptor (β-bungarotoxin binding protein) from muscle with myasthenic sera was negatively affected by treatment with sodium-metaperiodate, glucosidase and trypsin, where as no effect was seen on treatment with lipase. This provides evidence that purified presynaptic receptor (β-bungarotoxin binding protein) is a glycoprotein.
