Strong_1977_Prog.Clin.Biol.Res_15_227

Reference

Title : Selective enzymatic hydrolysis of nerve terminal phospholipids by beta-bungarotoxin: biochemical and morphological studies - Strong_1977_Prog.Clin.Biol.Res_15_227
Author(s) : Strong PN , Heuser JE , Kelly RB
Ref : Prog Clin Biol Res , 15 :227 , 1977
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.

PubMedSearch : Strong_1977_Prog.Clin.Biol.Res_15_227
PubMedID: 928454

Related information

Citations formats

Strong PN, Heuser JE, Kelly RB (1977)
Selective enzymatic hydrolysis of nerve terminal phospholipids by beta-bungarotoxin: biochemical and morphological studies
Prog Clin Biol Res 15 :227

Strong PN, Heuser JE, Kelly RB (1977)
Prog Clin Biol Res 15 :227