cobrotoxin and Thymoma

Cobrotoxin-binding protein was isolated by affinity chromatography from human thymoma which had been surgically removed from patients with myasthenia gravis. The protein was composed of polypeptides with a molecular mass of 40, 51, 65, and 74 kilodaltons as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulphate. Isoelectric focusing of the protein gave pI values of 5.2-5.6 and 11. This is the first report of the isolation of the protein from human thymoma. These findings suggest that the cobrotoxin-binding protein from human thymoma patients with myasthenia gravis has subunits similar to those of fish electric organs or mammalian muscles.

Topics: Adult; Chromatography, Affinity; Cobra Neurotoxin Proteins; Electrophoresis, Polyacrylamide Gel; Female; Humans; Male; Middle Aged; Molecular Weight; Myasthenia Gravis; Receptors, Cholinergic; Thymoma; Thymus Neoplasms