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Title: Selective enzymatic hydrolysis of nerve terminal phospholipids by beta-bungarotoxin: biochemical and morphological studies. Author: Strong PN, Heuser JE, Kelly RB. Journal: Prog Clin Biol Res; 1977; 15():227-49. PubMed ID: 928454. Abstract: beta-Bungarotoxin, a presynaptic protein neurotoxin isolated from the venom of the snake Bungarus multicinctus, modifies release of neurotransmitter at the neuromuscular junction. The toxin has a potent phospholipase activity toward both natural membranes and phospholipid liposomes. Studies of ionic requirements and selective chemical modification demonstrate that beta-bungarotoxin can only modify synaptic transmission under conditions in which the phospholipase is active. Morphological studies on frog cutaneous pectoris neuromuscular junctions incubated with beta-toxin and horseradish peroxidase-conjugated beta-toxin support the hypothesis that beta-toxin specifically interacts with presynaptic plasma membranes and selectively hydrolyzes nerve terminal phospholipids.[Abstract] [Full Text] [Related] [New Search]