Characterization of a Kunitz trypsin inhibitor with one disulfide bridge purified from Swartzia pickellii

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dc.contributor.authorCavalcanti, MDM
dc.contributor.authorOliva, MLV
dc.contributor.authorFritz, H.
dc.contributor.authorJochum, M.
dc.contributor.authorMentele, R.
dc.contributor.authorSampaio, M.
dc.contributor.authorCoelho, LCBB
dc.contributor.authorBatista, IFC
dc.contributor.authorSampaio, CAM
dc.contributor.institutionUniversidade Federal de Pernambuco (UFPE)
dc.contributor.institutionUniv Pernambuco
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Munich
dc.date.accessioned2016-01-24T12:33:16Z
dc.date.available2016-01-24T12:33:16Z
dc.date.issued2002-03-01
dc.description.abstractSwartzia pickellii is a Leguminosae that belongs to the Caesalpinioideae sub-family the Swartzia pickellii Trypsin Inhibitor (SWTI), a serine proteinase inhibitor was isolated from its seeds. SWTI is a single polypeptide chain protein and it's structure has 174 amino acid residues, it homologous to other Kunitz plant inhibitors, however shows some major differences: it contains only one disulfide bridge, instead two which are usually found in plant Kunitz inhibitors, and the SWTI reactive site does not contain the usual Arg or Lys residues at the putative reactive site (position 65). A glycosylation site was detected at Asn38 with 1188 kDa carbohydrate portion. the primary structure micro heterogeneity was found combining the sequence determination and mass spectrometry. Three forms of SWTI were actually defined: two glycosylated forms a 20,204 kDa (Arg 165) and 20,185 kDa (His 165) and one deglycosylated form 19,016 kDa (Arg 165), all of them contain a Met residue at position 130. (C) 2002 Elsevier Science (USA).en
dc.description.affiliationUniv Fed Pernambuco, Dept Bioquim, Recife, PE, Brazil
dc.description.affiliationUniv Pernambuco, Dept Bioquim, Recife, PE, Brazil
dc.description.affiliationEscola Paulista Med, Dept Bioquim, BR-04023 São Paulo, Brazil
dc.description.affiliationUniv Munich, Abt Klin Chem & Klin Biochem, Munich, Germany
dc.description.affiliationUnifespEscola Paulista Med, Dept Bioquim, BR-04023 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent635-639
dc.identifierhttp://dx.doi.org/10.1006/bbrc.2002.6436
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 291, n. 3, p. 635-639, 2002.
dc.identifier.doi10.1006/bbrc.2002.6436
dc.identifier.issn0006-291X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/26764
dc.identifier.wosWOS:000174202700031
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectSwartzia pickelliien
dc.subjectstructure and specificityen
dc.subjectblood coagulationen
dc.subjectplant Kunitz inhibitoren
dc.subjecttrypsin inhibitoren
dc.subjecthuman plasma kallikreinen
dc.subjectplasminen
dc.subjectprimary structure determinationen
dc.titleCharacterization of a Kunitz trypsin inhibitor with one disulfide bridge purified from Swartzia pickelliien
dc.typeinfo:eu-repo/semantics/article
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