Amino Acid Sequence of a Neurotoxic Phospholipase A2 Enzyme From Common Death Adder (Acanthophis antarcticus) Venom

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dc.contributor.author Van Der Weyden Lex en_US
dc.contributor.author Hains Peter en_US
dc.contributor.author Broady Kevin en_US
dc.contributor.author Shaw Denis en_US
dc.contributor.author Milburn Peter en_US
dc.date.accessioned 2010-05-14T07:45:12Z
dc.date.available 2010-05-14T07:45:12Z
dc.date.created 2010-05-14T07:45:12Z en_US
dc.date.issued 2001
dc.identifier 2004004338 en_US
dc.identifier.citation Van Der Weyden Lex et al. 2001, 'Amino Acid Sequence of a Neurotoxic Phospholipase A2 Enzyme From Common Death Adder (Acanthophis antarcticus) Venom', Alaken Inc., vol. 10, no. 1, pp. 33-42. en_US
dc.identifier.issn 1058-8108 en_US
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/6220
dc.description.abstract The amino acid sequence of the first neurotoxic phospholipase A2, acanthoxin AI, purified from the venom of the Common death adder (Acanthophis antarcticus) was determined. Acanthoxin Al shows high homology with other Australian elapid PLA2 neurotoxins, in particular Acanthin -I and -II, also from Death adder, Pseudexin A from the Red-bellied black snake (Pseudechis porphyriacus), and Pa-I2a and Pa-9c from the King brown snake (Pseudechis australis). Acanthoxin Al is a single-chain 118 amino acid residue PLA2, including 14 half cystine residues and the essential residues forming the ubiquitous calcium binding pocket and catalytic site. Critical analysis of the residues hypothesized to be important for neurotoxicity is presented. en_US
dc.publisher Alaken Inc. en_US
dc.relation.isbasedon en_US
dc.title Amino Acid Sequence of a Neurotoxic Phospholipase A2 Enzyme From Common Death Adder (Acanthophis antarcticus) Venom en_US
dc.parent Journal for Natural Toxins en_US
dc.journal.volume 10 en_US
dc.journal.number 1 en_US
dc.publocation USA en_US
dc.identifier.startpage 33 en_US
dc.identifier.endpage 42 en_US
dc.cauo.name Cell and Molecular Biology en_US
dc.for 110705 en_US


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