Fate of alpha-bungarotoxin bound to acetylcholine receptors of normal and denervated muscle.
In organ culture, alpha-[(125)I]bungarotoxin bound to extrajunctional receptors of denervated muscle is lost from the tissue at a more rapid rate than the toxin bound to the junctional receptors of normal muscle. The rapid loss of toxin from denervated muscle can be blocked by inhibitors of energy production and protein synthesis, and may reflect turnover of the toxin-receptor complex in the membrane.
D000818:Animals; D001665:Binding Sites; D002038:Bungarotoxins / Q000378:metabolism*; D003513:Cycloheximide / Q000494:pharmacology; D003964:Diaphragm; D007457:Iodine Radioisotopes; D007700:Kinetics; D009121:Muscle Denervation; D009124:Muscle Proteins / Q000096:biosynthesis; D009132:Muscles / Q000294:innervation / Q000378:metabolism*; D009469:Neuromuscular Junction / Q000378:metabolism; D009924:Organ Culture Techniques; D011691:Puromycin / Q000494:pharmacology; D051381:Rats; D011950:Receptors, Cholinergic / Q000187:drug effects*
D002038:Bungarotoxins; D007457:Iodine Radioisotopes; D009124:Muscle Proteins; D011950:Receptors, Cholinergic; D011691:Puromycin; D003513:Cycloheximide