Toxin assay

Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues – 6 to 7 amino acid residues in defined sequence

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Details

435 71, 435 74, A61K 3804, G01N 3353, G01N 33573

Patent

active

059626372

ABSTRACT:
A toxin assay that uses a substrate for cleavage by the toxin and antibodies that do not recognise the substrate but recognise and bind to the product of cleavage of the substrate by the toxin. The substrate can be a nerve cell peptide when the assay is for botulinum toxin or tetanus toxin.

REFERENCES:
patent: 5171662 (1992-12-01), Sharma
Oyler, G.A. et al., "The Indentification of a Novel Synaptosomal-associated Protein, SNAP-25, Differentially Expressed by Neuronal Subpopulations," J. Cell Bio . 109:3039-3052 (1989).
Schiavo et al. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin, Nature, vol. 359, pp. 832-835, see abstract, p. 832, col. 2, paragraph 1, p. 833, col. 2, paragraph 1 and Figure 3, Oct. 1992.
Sollner et al., SNAP receptors implicated in vesicle targeting and fusion, Nature, vol. 352, pp. 318-324, see abstract and Figure 3, Mar. 1993.
Foran, P. et al., "Differences in the Protease Activities of Tetanus and Botulinum B Toxins Revealed by the Cleavage of Vesicle-Associated Membrane Protein and Various Sized Fragments," Biochem . 33:15365-15374 (Dec. 27, 1994).
Rossetto, O. et al., "SNARE Motif and Neurotoxins, " Nature 372:415-416 (Dec. 1, 1994).
Shone, C. and Roberts, A., "Peptide Substrate Specificity and Properties of the Zinc-Endopeptidase Activity of Botulinum Type B Neurotoxin," Eur. J. Biochem . 225:263-270 (Oct. 1, 1994).

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