dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorTakeda, AAS
dc.creatordos Santos, J. I.
dc.creatorMarcussi, S.
dc.creatorSilveira, L. B.
dc.creatorSoares, A. M.
dc.creatorFontes, MRM
dc.date2014-05-20T13:49:20Z
dc.date2016-10-25T17:01:50Z
dc.date2014-05-20T13:49:20Z
dc.date2016-10-25T17:01:50Z
dc.date2004-06-01
dc.date.accessioned2017-04-05T21:01:02Z
dc.date.available2017-04-05T21:01:02Z
dc.identifierBiochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1699, n. 1-2, p. 281-284, 2004.
dc.identifier1570-9639
dc.identifierhttp://hdl.handle.net/11449/17577
dc.identifierhttp://acervodigital.unesp.br/handle/11449/17577
dc.identifier10.1016/j.bbapap.2004.02.005
dc.identifierWOS:000221807800030
dc.identifierhttp://dx.doi.org/10.1016/j.bbapap.2004.02.005
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/864027
dc.descriptionAn acidic phospholipase A(2) (PLA(2)) isolated from Bothrops jararacussu snake venom was crystallized with two inhibitors: alpha-tocopherol (vitamin E) and p-bromophenacyl bromide (BPB). The crystals diffracted at 1.45- and 1.85-Angstrom resolution, respectively, for the complexes with alpha-tocopherol and p-bromophenacyl bromide. The crystals are not isomorphous with those of the native protein, suggesting the inhibitors binding was successful and changes in the quaternary structure may have occurred. (C) 2004 Elsevier B.V. All rights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationBiochimica et Biophysica Acta: Proteins and Proteomics
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectcrystallization
dc.subjectX-ray crystallography
dc.subjectacidic phospholipase A(2)
dc.subjectBothrops jararacussu venom
dc.subjectalpha-tocopherol
dc.subjectp-bromophenacyl bromide
dc.titleCrystallization and preliminary X-ray diffraction analysis of an acidic phospholipase A(2) complexed with p-bromophenacyl bromide and alpha-tocopherol inhibitors at 1.9-and 1.45-A resolution
dc.typeOtro


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