In vitro neuromuscular activity of snake venoms

  title={In vitro neuromuscular activity of snake venoms},
  author={Wayne C. Hodgson and Janith Chatura Wickramaratna},
  journal={Clinical and Experimental Pharmacology and Physiology},
1. Snake venoms consist of a multitude of pharmacologically active components used for the capture of prey. Neurotoxins are particularly important in this regard, producing paralysis of skeletal muscles. These neurotoxins can be classified according to their site of action (i.e. pre‐ or post‐synaptic). 
Inhibition of Hemorragic Snake Venom Components: Old and New Approaches
A deeper knowledge of alternative ways to inhibit venom toxins may provide supplemental treatments to serum therapy, and direct electric current from low voltage showed neutralizing properties against venom phospholipase A2 and metalloproteases.
[The composition, biochemical properties and toxicity of snake venoms].
All snake venoms are grouped depending on their mode of action, and usually cause neurotransmission disorders, cardiotoxic action, hemostasis disorders, and have central nervous system and necrotic activity.
Presynaptic neurotoxins with enzymatic activities.
This work focuses on presynaptic neurotoxins, which are very potent inhibitors of the neurotransmitter release because they are endowed with specific enzymatic activities: (1) clostridial neurotoxin with a metallo-proteolytic activity and (2).
Snake venoms and their toxins: an Australian perspective.
Neuromuscular activity of Bothrops alcatraz snake venom in chick biventer cervicis preparations.
Preliminary Results of the in Vivo and in Vitro Characterization of a Tentacle Venom Fraction from the Jellyfish Aurelia aurita
Electrophysiological characterization demonstrated that one of these fractions potently inhibited ACh-elicited currents mediated by both vertebrate fetal and adult muscle nicotinic acetylcholine receptors (nAChR) subtypes.
Snake Venom: Any Clue for Antibiotics and CAM?
It is shown that snake venoms are not totally unexplored sources for antibiotics and complementary and alternative medicine (CAM) and how the microorganisms can be resistant to antibiotics is shown.
In vitro neurotoxic effects of Pseudechis spp. venoms: A comparison of avian and murine skeletal muscle preparations.
In vitro comparison of enzymatic effects among Brazilian Bothrops spp. venoms.


Use of a snake venom toxin to characterize the cholinergic receptor protein.
  • J. Changeux, M. Kasai, C. Lee
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1970
alpha-Bungarotoxin, a polypeptide of mol wt 8000 purified from the venom of Bungarus multicinctus, blocks irreversibly and specifically the excitation by cholinergic agonists on the isolated
Snake venom alpha-neurotoxins and other 'three-finger' proteins.
  • V. Tsetlin
  • Biology, Chemistry
    European journal of biochemistry
  • 1999
The main emphasis is placed on recent data characterizing the alpha-neurotoxin interactions with nicotinic acetylcholine receptors.
The Neurotoxicity of the Venom Phospholipases A2, Notexin and Taipoxin
The presynaptically active, toxic phospholipases known as notexin and taipoxin are principal components of the venom of the Australian tiger snake and the Australian taipan respectively. The
Purification of a presynaptic neurotoxin from the venom of the australian tiger snake Notechis scutatus scutatus.
Neuromuscular effects of four phospholipases A2 from the venom of Pseudechis australis, the Australian king brown snake.
Taipoxin, an extremely potent presynaptic neurotoxin from the venom of the australian snake taipan (Oxyuranus s. scutellatus). Isolation, characterization, quaternary structure and pharmacological properties.
Taipoxin (taipan toxin), purified from the venom of the Australian taipan (Oxyuranus s. scutellatus) by gel filtration on Sephadex G-75 followed by column zone electrophoresis, is the most lethal
Presynaptic effects of snake venom toxins which have phospholipase A2 activity (beta-bungarotoxin, taipoxin, crotoxin).
  • M. Su, C. Chang
  • Biology, Chemistry
    Toxicon : official journal of the International Society on Toxinology
  • 1984
Crotoxin, the neurotoxin of South American rattlesnake venom, is a presynaptic toxin acting like β-bungarotoxin
The effects of crotoxin are very similar to those of β-bungarotoxin and most likely due to the presynaptic inhibition of the mechanism mediating the release of neurotransmitter in the nerve terminal.