Abstract
Antisera were raised against the presynaptic neurotoxin β-bungarotoxin and against its phospholipase-inactive derivative, modified by reaction with
p
-bromophenacyl bromide. The cross-reactivity of the antisera to other phospholipase A
2
enzymes and polypeptide neurotoxins was examined. The antisera inhibited both the neurotoxic effects of β-bungarotoxin at the frog motor endplate and the enzymatic activity of the toxin on model phospholipid membranes, although it is unlikely that the catalytic active centre is the locus of any major determinant.
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