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Primary structure of gamma-bungarotoxin, a new postsynaptic neurotoxin from venom of Bungarus multicinctus

Academic Article
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Overview

authors

  • Aird, S. D.
  • Womble, G. C.
  • Yates III, John
  • Griffin, Patrick

publication date

  • April 1999

journal

  • Toxicon  Journal

abstract

  • The primary structure of gamma-bungarotoxin, a new toxin from Bungarus multicinctus venom, was determined using mass spectrometry and Edman degradation. The toxin has a mass of 7524.7 D and consists of 68 residues having the following sequence: MQCKTCSFYT CPNSETCPDG KNICVKRSWT AVRGDGPKRE IRRECAATCP PSKLGLTVFC CTTDNCNH. Gamma-bungarotoxin is structurally similar to both kappa-bungarotoxin and elapid long postsynaptic neurotoxins. Its C-terminal nine residues are identical to those of the kappa-toxins. Its disulfide bond locations appear identical to those of several elapid toxins of unknown pharmacology and its hydrophobicity profile is also strikingly similar. However, with an LD50 of 0.15 microg/g i.v. in mice, gamma-bungarotoxin is 30-150-fold more toxic than other members of this latter class. Its toxicity is comparable to those of alpha-nicotinic acetylcholine receptor antagonists.

subject areas

  • Amino Acid Sequence
  • Animals
  • Bungarotoxins
  • Bungarus
  • Chromatography
  • Chromatography, High Pressure Liquid
  • Injections, Intraventricular
  • Male
  • Mass Spectrometry
  • Mice
  • Molecular Sequence Data
  • Neurotoxins
  • Receptors, Neurotransmitter
  • Solubility
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Research

keywords

  • disulfide bond positions
  • hydrophobicity
  • postsynaptic neurotoxin
  • primary structure
  • snake venom
  • toxicity
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Identity

International Standard Serial Number (ISSN)

  • 0041-0101

Digital Object Identifier (DOI)

  • 10.1016/s0041-0101(98)00199-8

PubMed ID

  • 10082161
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Additional Document Info

start page

  • 609

end page

  • 625

volume

  • 37

issue

  • 4

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