Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.M414137200
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dc.titleOhanin, a novel protein from king cobra venom, induces hypolocomotion and hyperalgesia in mice
dc.contributor.authorYuh, F.P.
dc.contributor.authorWong, P.T.H.
dc.contributor.authorKumar, P.P.
dc.contributor.authorHodgson, W.C.
dc.contributor.authorKini, R.M.
dc.date.accessioned2014-10-27T08:35:13Z
dc.date.available2014-10-27T08:35:13Z
dc.date.issued2005-04-01
dc.identifier.citationYuh, F.P., Wong, P.T.H., Kumar, P.P., Hodgson, W.C., Kini, R.M. (2005-04-01). Ohanin, a novel protein from king cobra venom, induces hypolocomotion and hyperalgesia in mice. Journal of Biological Chemistry 280 (13) : 13137-13147. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M414137200
dc.identifier.issn00219258
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101256
dc.description.abstractWe have identified, purified, and determined the complete amino acid sequence of a novel protein, ohanin from Ophiophagus hannah (king cobra) venom. It is a small protein containing 107 amino acid residues with a molecular mass of 11951.47 ± 0.67 Da as assessed by electrospray ionization-mass spectrometry. It does not show similarity to any known families of snake venom proteins and hence is the first member of a new family of snake venom proteins. It shows similarity to PRY and SPRY domain proteins. It is nontoxic up to 10 mg/kg when injected intraperitoneally in mice. Ohanin produced statistically significant and dose-dependent hypolocomotion in mice. In a pain threshold assay, it showed dose-dependent hyperalgesic effect. The ability of the protein to elicit a response at greatly reduced doses when injected intracerebroventricularly as compared with intraperitoneal administration in both the locomotion and hot plate experiments strongly suggests that ohanin acts on the central nervous system. Since the natural abundance of the protein in the venom is low (∼1 mg/g), a synthetic gene was constructed and expressed. The recombinant protein, which was obtained in the insoluble fraction in Escherichia coli, was purified under denaturing condition and was refolded. Recombinant ohanin is structurally and functionally similar to native protein as determined by circular dichroism and hot plate assay, suggesting that it will be useful in future structure-function relationship studies. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1074/jbc.M414137200
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1074/jbc.M414137200
dc.description.sourcetitleJournal of Biological Chemistry
dc.description.volume280
dc.description.issue13
dc.description.page13137-13147
dc.description.codenJBCHA
dc.identifier.isiut000227922000125
Appears in Collections:Staff Publications

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