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Green mamba

Fasciculin 4 Dendroaspis viridis (western green mamba)... [Pg.145]

The fasciculins are a family of closely related peptides that are isolated from the venom of mambas and exert their toxic action by inhibiting AChE. The crystal structure of fasciculin 2 from green mamba Dendroaspis angusticeps) snake venom was first resolved in 1992 (Le Du et al., 1992). The three-dimensional (3D) structure of fasciculin 1 obtained from the US National Library of Medicine, National Center for Biotechnology Information, MMDB database is illustrated in Figure 11.2. [Pg.145]

Lee, C.Y., Lee S-Y., Chen, Y.M. (1986). A study on the cause of death produced by angusticeps-type toxin F7 isolated from eastern green mamba venom. Toxicon 24 33-40. [Pg.152]

Dajas, F., Bolioli, B., Castello, M.E., Silveira, R. (1987). Rat striatal acetylcholinesterase inhibition by fasciculin (a polypeptide fi-om green mamba snake venom). Neurosci. Lett. 77 87-91. [Pg.475]

Acetylcholine receptors - muscarinic agonists There are a number of natural plant alkaloid toxins, including arecoline, muscarine and pilocarpine and green mamba snake peptides venoms, including MTl, MT2, MTS and MT4. [Pg.195]

Common Name(s) Western Dendroaspis Jamesoni Kaimosae Green Mamba... [Pg.74]

Amino acid polypeptide toxin from Eastern green mamba (Dendroaspis augusticeps). Inhibits potassium channels and facilitates release of ACh at nerve terminals increases evoked release but does not produce spontaneous release of ACh. [Pg.677]

Finally, venoms from different snakes from the Elapidae and Hydrophidae families also contain a cocktail of different paralytic toxins, some of which are selective for voltage-dependent Ca channels. For instance, the venom of the black mamba Dendroaspis polylepis polylepis contains a toxin termed calciseptine, which selectively blocks L-type Ca channels [6] and the venom from the green mamba D. agusticeps contains calcicludine, a toxin that acts as a potent blocker of most of the HVA Ca channels [7]. [Pg.110]

Harvey, A., and Karlsson, E. (1980). Dendrotoxin from the Venom of the Green Mamba, Dendroaspis angusti-ceps" Naunyn-Schmiedebergs Arch. Pharmacol. 312 1-6. [Pg.118]

A neurotoxin with 59 amino acid units from Dendro-aspis angusticeps (African green mamba) Mr 7071. It blocks presynaptic K channels (IC50 ca. 15 nM) of various neurons and increases neuromuscular transmission. This is achieved by an increased liberation of acetylcholine at the neuromuscular branching points. An elevated liberation of neurotransmitters due to binding to a membrane-associated protein receptor has been observed (guinea pigs). To date a-, /5-, y-, and 6-D. have been described. [Pg.178]

FIGURE 30.2 The 3-D protein structure of Fasl derived from green mamba (D. angusticeps) snake venom. Source Image obtained from the public domain at the US National Library of Medicine, Natiorud Center for Biotechnology Information, MMDB. [Pg.414]

Le Du, M.H., Marchot, R, Bougis, R, et al., 1992. 1.9-A Resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom. J. Biol. Chem. 267, 22122-22130. [Pg.419]

Anderson, A. J., Harvey, A. L., and Mbugua, P. M. (1985). Effects of fasciculin 2, an anticholinesterase polypeptide from green mamba venom, on neuromuscular transmission in mouse diaphragm preparations. Neurosci. Lett. 54 123-128. [Pg.58]

Benishin, C. G., Sorensen, R. G., Brown, W. E., Krueger, B. K., and Blaustein, M. P. (1988). Four polypeptide components of green mamba venom selectively block certain potassium channels in rat brain synaptosomes. Mol. Pharmacol. 34 152-159. [Pg.58]

Karlsson, E. D., Mbugua, R, and Rodriquez-Ithurralde, D. (1984). Fasciculins, anticholinesterase toxins from the venom of green mamba Dendroaspis angusticeps. Pharmacol Ther. 30 259-276. [Pg.60]

Menez, R., and Ducruix, A. (1990). Rreliminary x-ray analysis of crystals of fasciculin 1, a potent acetylcholinesterase inhibitor from green mamba venom. J. Mol Biol 216 233-234. [Pg.60]


See other pages where Green mamba is mentioned: [Pg.795]    [Pg.17]    [Pg.290]    [Pg.447]    [Pg.795]    [Pg.145]    [Pg.145]    [Pg.145]    [Pg.465]    [Pg.467]    [Pg.482]    [Pg.482]    [Pg.93]    [Pg.329]    [Pg.75]    [Pg.30]    [Pg.413]    [Pg.413]    [Pg.413]    [Pg.60]   
See also in sourсe #XX -- [ Pg.17 ]




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