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pubmed-article:12056805pubmed:abstractTextA neurotoxin, Oh9-1, from the venom of Ophiophagus hannah was isolated by a combination of ion-exchange chromatography and reverse phase HPLC. Amino acid sequence analysis revealed that Oh9-1 consists of 57 amino acids and eight cysteine residues. This protein was mainly constituted with beta-sheet as evidenced by CD spectrum. Oh9-1 inhibited carbachol-induced muscle contraction in an irreversible manner and the dose for achieving 50% inhibition was approximately fourfold that of alpha-bungarotoxin. Since the residues in alpha-neurotoxins closely involve in the binding with acetylcholine receptors are not highly conserved in this toxin molecule, Oh9-1 represents a novel type of neurotoxin structurally distinct from alpha-neurotoxins.lld:pubmed
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pubmed-article:12056805pubmed:authorpubmed-author:LinShinne-Ren...lld:pubmed
pubmed-article:12056805pubmed:authorpubmed-author:ChangLong-Sen...lld:pubmed
pubmed-article:12056805pubmed:authorpubmed-author:LiouJau-Cheng...lld:pubmed
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pubmed-article:12056805pubmed:dateRevised2007-11-15lld:pubmed
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pubmed-article:12056805pubmed:year2002lld:pubmed
pubmed-article:12056805pubmed:articleTitlePurification and characterization of a neurotoxin from the venom of Ophiophagus hannah (king cobra).lld:pubmed
pubmed-article:12056805pubmed:affiliationInstitute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung 804, Taiwan. lschang@mail.nsysu.edu.twlld:pubmed
pubmed-article:12056805pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12056805pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed