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• W2044080354 abstract "1 A homogeneous preparation of botulinum neurotoxin from Clostridium botulinum type A was labelled with [125I]iodine to high specific activity (e.g. 1750 Ci/mmol) with chloramine-T and shown to retain appreciable biological activity (e. g. 1.2 × 108 mouse LD50/mg). 2 Both of the toxin's subunits were iodinated as shown by sodium dodecyl sulphate gel electrophoresis; the behaviour of native and labelled toxin on Ouchterlony double immunodiffusion was identical. 3 Saturable binding of the 125I-labelled neurotoxin to rat brain synaptosomal membranes was demonstrated. A small fraction of these sites (60 fmol/mg protein) exhibited high affinity for the toxin (Kd= 0.6 nM) whilst the majority displayed a much weaker affinity. Kinetic analyses of the interaction of toxin with synaptosomes were found to be complex, consistent with the existence of heterogeneity. 4 Treatment of the membranes with proteases or heating prevented all the specific binding, suggesting the involvement of protein component(s). In addition, the ability of neuraminidase, and to a lesser extent gangliosides, to reduce the extent of binding to both the high-affinity and low-affinity sites, suggests the involvement of sialic residues in toxin binding. 5 The two individual subunits of native neurotoxin were separated and renatured; only the larger (Mr 97000) competed with the binding of labelled neurotoxin. Tetanus toxin was capable of decreasing the binding, albeit with low efficacy. 6 The binding component(s) appear selective as binding was unaltered by botulinum type B neurotoxin, other pure presynaptically-active neurotoxins (α-latrotoxin, β-bungarotoxin or dendrotoxin) and known antagonists of botulism. Taipoxin, crotoxin and bee venom phospholipase A2 did inhibit the binding; however, their relatively low potencies, which are decreased further in the absence of their phospholipase A2 activity, indicate a non-specific mechanism. 7 The function of the membraneous toxin binding component(s) is discussed in relation to the molecular basis of the neurotoxin's action." @default.
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• W2044080354 date "1983-03-01" @default.
• W2044080354 modified "2023-09-24" @default.
• W2044080354 title "Radioiodination of Botulinum Neurotoxin Type A with Retention of Biological Activity and Its Binding to Brain Synaptosomes" @default.
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• W2044080354 doi "https://doi.org/10.1111/j.1432-1033.1983.tb07282.x" @default.
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