Effect of phospholipase C on the binding of alpha-bungarotoxin to isolated plasma membranes of rat skeletal muscle.
Sarcolemmal membranes were isolated from hindlimb muscles of the rat and the specific binding of [125I]alpha-bungarotoxin to the membranes was determined. Incubation of the membranes with a purified preparation of phospholipase C (ex Clostridium perfringens) increased the specific binding of the toxin (Bmax). The apparent dissociation constant (Kd) for the binding was unchanged by treatment with the enzyme. The possibility that latent acetylcholine receptors exist in muscle sarcolemma, and that these receptors can be activated by the enzyme, is discussed.
D000109:Acetylcholine / Q000494:pharmacology; D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D002038:Bungarotoxins / Q000378:metabolism*; D008297:Male; D009132:Muscles / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D012508:Sarcolemma / Q000378:metabolism; D010738:Type C Phospholipases / Q000494:pharmacology*
D002038:Bungarotoxins; D010738:Type C Phospholipases; D000109:Acetylcholine