%0 Journal Article
%T Purification of Beta Bungarotoxin (¦Â-Bgtx) Binding Protein from Human Cadaver Skeletal Muscle
%A Suhail Rasool
%A B.L. Jailkhani
%A M. Irshad
%A Madhuri Behari
%J Journal of Medical Sciences
%D 2007
%I 
%X High affinity ¦Â-bungarotoxin binding protein was purified from skeletal muscle of human cadaver by affinity chromatography using ¦Â-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¡À0.15 nmoles and binding sites of 34¡À2.3 f mole/mg tissue. Immunoreactivity profile of purified presynaptic receptor (¦Â-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 (¦Â-bungarotoxin binding protein) is a glycoprotein.
%K skeletal muscle
%K purification
%K immunoreactivity
%K B-bungarotoxin
%U http://docsdrive.com/pdfs/ansinet/jms/2007/195-202.pdf