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dc.creatorFrancis, Brian
dc.creatorGutiérrez, José María
dc.creatorLomonte, Bruno
dc.creatorKaiser, Ivan I.
dc.date.accessioned2016-11-09T20:50:33Z
dc.date.available2016-11-09T20:50:33Z
dc.date.issued1991
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/0003986191903075es_ES
dc.identifier.issn0003-9861
dc.identifier.urihttp://hdl.handle.net/10669/29165
dc.description.abstractA basic, dimeric myotoxic protein, myotoxin II, purified from Bothrops asper venom has a similar molecular weight and is immunologically cross-reactive with antibodies raised to previously isolated B. asper phospholipases A2, except that it shows only 0.1% of the phospholipase activity against L-alpha-phosphatidylcholine in the presence of Triton X-100. Its 121 amino acid sequence, determined by automated Edman degradation, clearly identifies it as a Lys-49 phospholipase A2. Key amino acid differences between myotoxin II and phospholipase active proteins in the Ca2(+)-binding loop region, include Lys for Asp-49, Asn for Tyr-28, and Leu for Gly-32. The latter substitution has not previously been seen in Lys-49 proteins. Other substitutions near the amino terminus (Leu for Phe-5 and Gln for several different amino acids at position 11) may prove useful for identifying other Lys-49 proteins in viperid and crotalid venoms. Myotoxin II shows greater sequence identity with other Lys-49 proteins from different snake venoms (Agkistrodon piscivorus piscivorus, Bothrops atrox, and Trimeresurus flavoviridis) than with another phospholipase A2 active Asp-49 molecule isolated from the same B. asper venom. This work demonstrates that phospholipase activity per se, is not required in phospholipase molecules for either myotoxicity or edema inducing activities.es_ES
dc.language.isoen_USes_ES
dc.sourceArchives of Biochemistry and Biophysics. Volumen 284, Número 2, 1991es_ES
dc.subjectAmino Acid Sequencees_ES
dc.subjectAnimalses_ES
dc.subjectAntibodieses_ES
dc.subjectCalciumes_ES
dc.subjectCattlees_ES
dc.subjectCross Reactionses_ES
dc.subjectCrotalid Venomses_ES
dc.subjectGroup II Phospholipases A2es_ES
dc.subjectHumanses_ES
dc.subjectLysinees_ES
dc.subjectMolecular Sequence Dataes_ES
dc.subjectNeurotoxinses_ES
dc.subjectOctoxynoles_ES
dc.subjectPhospholipases Aes_ES
dc.subjectPhospholipases A2es_ES
dc.subjectPolyethylene Glycolses_ES
dc.subjectProtein Conformationes_ES
dc.subjectRatses_ES
dc.subjectReptilian Proteinses_ES
dc.subjectSnake venomes_ES
dc.titleMyotoxin II from Bothrops asper (Terciopelo) venom is a lysine-49 phospholipase A2es_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1016/0003-9861(91)90307-5
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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