Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194174
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dc.contributor.CRUESPUNIVERSIDADE DE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleThe Amino Acid Sequence Of Bothropstoxin-ii, An Asp-49 Myotoxin From Bothrops Jararacussu (jararacucu) Venom With Low Phospholipase A2 Activity.pt_BR
dc.contributor.authorPereira, M Fpt_BR
dc.contributor.authorNovello, J Cpt_BR
dc.contributor.authorCintra, A Cpt_BR
dc.contributor.authorGiglio, J Rpt_BR
dc.contributor.authorLanducci, E Tpt_BR
dc.contributor.authorOliveira, Bpt_BR
dc.contributor.authorMarangoni, Spt_BR
unicamp.authorM F Pereira, Department of Biochemistry, Institute of Biology, UNICAMP, Campinas-SP, Brazil.pt_BR
unicamp.author.externalJ C Novello,pt
unicamp.author.externalA C Cintra,pt
unicamp.author.externalJ R Giglio,pt
unicamp.author.externalE T Landucci,pt
unicamp.author.externalB Oliveira,pt
unicamp.author.externalS Marangoni,pt
dc.subjectAmino Acid Sequencept_BR
dc.subjectAnimalspt_BR
dc.subjectAspartic Acidpt_BR
dc.subjectBothropspt_BR
dc.subjectChromatography, High Pressure Liquidpt_BR
dc.subjectCrotalid Venomspt_BR
dc.subjectElectrophoresis, Polyacrylamide Gelpt_BR
dc.subjectGroup Ii Phospholipases A2pt_BR
dc.subjectHydrolysispt_BR
dc.subjectMolecular Sequence Datapt_BR
dc.subjectPhospholipases Apt_BR
dc.subjectPhospholipases A2pt_BR
dc.subjectReptilian Proteinspt_BR
dc.subjectSerine Endopeptidasespt_BR
dc.description.abstractThe complete amino acid sequence of bothropstoxin-II (BthTX-II), a myotoxin isolated from Bothrops jararacussu snake venom, is reported. The results show that BthTX-II is an Asp-49 phospholipase A2 (PLA2)-like protein composed of a single polypeptide chain of 120 amino acid residues (Mr = 13,976), containing one methionine and 14 half-cystines. Despite a high degree of homology with other PLA2's and the presence of the strategic residues known to compose the Ca2+-binding loop, namely Tyr-28, Gly-30, Gly-32, and especially Asp-49, besides His-48, Tyr-52, and Asp-99, all of them directly or indirectly involved in catalysis, BthTX-II revealed a very low PLA2 activity when assayed on egg yolk phosphatidylcholine. We attribute this low catalytic activity to the existence of extra mutations, e.g., Trp-5 for Phe-5, which points to the need of considering other strategic positions, since only Lys-49 PLA2's have been considered to be devoid of this enzymatic activity.en
dc.relation.ispartofJournal Of Protein Chemistrypt_BR
dc.relation.ispartofabbreviationJ. Protein Chem.pt_BR
dc.date.issued1998-Maypt_BR
dc.identifier.citationJournal Of Protein Chemistry. v. 17, n. 4, p. 381-6, 1998-May.pt_BR
dc.language.isoengpt_BR
dc.description.volume17pt_BR
dc.description.firstpage381-6pt_BR
dc.rightsfechadopt_BR
dc.rights.holderpt_BR
dc.sourcePubMedpt_BR
dc.identifier.issn0277-8033pt_BR
dc.identifier.doipt_BR
dc.identifier.urlhttp://www.ncbi.nlm.nih.gov/pubmed/9619591pt_BR
dc.date.available2015-11-27T12:19:14Z-
dc.date.accessioned2015-11-27T12:19:14Z-
dc.description.provenanceMade available in DSpace on 2015-11-27T12:19:14Z (GMT). No. of bitstreams: 1 pmed_9619591.pdf: 764391 bytes, checksum: 42c0d8f62c311147eb5eec2b362f638c (MD5) Previous issue date: 1998en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194174-
dc.identifier.idPubmed9619591pt_BR
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