Purification of a PHA-Like chitin-binding protein from Acacia farnesiana seeds: A time-dependent oligomerization protein

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dc.contributor.authorSanti-Gadelha, T.
dc.contributor.authorRocha, B. A. M.
dc.contributor.authorOliveira, C. C.
dc.contributor.authorAragao, K. S.
dc.contributor.authorMarinho, E. S.
dc.contributor.authorGadelha, C. A. A.
dc.contributor.authorToyama, M. H. [UNESP]
dc.contributor.authorPinto, V. P. T.
dc.contributor.authorNagano, C. S.
dc.contributor.authorDelatorre, P.
dc.contributor.authorMartins, J. L.
dc.contributor.authorGalvani, F. R.
dc.contributor.authorSampaio, A. H.
dc.contributor.authorDebray, H.
dc.contributor.authorCavada, B. S.
dc.contributor.institutionUniversidade Federal da Paraíba (UFPB)
dc.contributor.institutionUniversidade Federal do Ceará (UFC)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniv Reg Cariri
dc.contributor.institutionUniversidade Federal de Pelotas (UFPEL)
dc.contributor.institutionUniv Sci & Technol
dc.date.accessioned2014-05-20T15:32:31Z
dc.date.available2014-05-20T15:32:31Z
dc.date.issued2008-07-01
dc.description.abstractA lectin-like protein from the seeds of Acacia farnesiana was isolated from the albumin fraction, characterized, and sequenced by tandem mass spectrometry. The albumin fraction was extracted with 0.5 M NaCl, and the lectin-like protein of A. farnesiana (AFAL) was purified by ion-exchange chromatography (Mono-Q) followed by chromatofocusing. AFAL agglutinated rabbit erythrocytes and did not agglutinate human ABO erythrocytes either native or treated with proteolytic enzymes. In sodium dodecyl sulfate gel electrophoresis under reducing and nonreducing conditions, AFAL separated into two bands with a subunit molecular mass of 35 and 50 kDa. The homogeneity of purified protein was confirmed by chromatofocusing with a pI=4.0+/-0.5. Molecular exclusion chromatography confirmed time-dependent oligomerization in AFAL, in accordance with mass spectrometry analysis, which confers an alteration in AFAL affinity for chitin. The protein sequence was obtained by a liquid chromatography quadrupole time-of-flight experiment and showed that AFAL has 68% and 63% sequence similarity with lectins of Phaseolus vulgaris and Dolichos biflorus, respectively.en
dc.description.affiliationUniversidade Federal da Paraíba (UFPB), Dept Biol, BR-58059900 Joao Pessoa, Paraiba, Brazil
dc.description.affiliationUniversidade Federal do Ceará (UFC), Dept Bioquim & Biol Mol, BioMol Lab, Fortaleza, Ceara, Brazil
dc.description.affiliationUniv Estadual Paulista, São Paulo, Brazil
dc.description.affiliationUniversidade Federal do Ceará (UFC), Fac Med Sobral, Sobral, Brazil
dc.description.affiliationUniv Reg Cariri, Dept Ciencias Fis & Biol, Crato, Brazil
dc.description.affiliationUniv Fed Pelotas, IQG, Pelotas, RS, Brazil
dc.description.affiliationUniversidade Federal do Ceará (UFC), Dept Engn Pesca, Fortaleza, Ceara, Brazil
dc.description.affiliationUniv Sci & Technol, Lille, France
dc.description.affiliationUnespUniv Estadual Paulista, São Paulo, Brazil
dc.format.extent97-111
dc.identifierhttp://dx.doi.org/10.1007/s12010-008-8144-0
dc.identifier.citationApplied Biochemistry and Biotechnology. Totowa: Humana Press Inc, v. 150, n. 1, p. 97-111, 2008.
dc.identifier.doi10.1007/s12010-008-8144-0
dc.identifier.issn0273-2289
dc.identifier.lattes8573195327542061
dc.identifier.urihttp://hdl.handle.net/11449/41401
dc.identifier.wosWOS:000256962600008
dc.language.isoeng
dc.publisherHumana Press Inc
dc.relation.ispartofApplied Biochemistry and Biotechnology
dc.relation.ispartofjcr1.797
dc.relation.ispartofsjr0,571
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectAcacia farnesianaen
dc.subjectlectin-like proteinen
dc.subjectpurificationen
dc.subjectoligomerizationen
dc.subjecttandem mass spectrometryen
dc.titlePurification of a PHA-Like chitin-binding protein from Acacia farnesiana seeds: A time-dependent oligomerization proteinen
dc.typeArtigo
dcterms.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dcterms.rightsHolderHumana Press Inc
unesp.author.lattes8573195327542061
unesp.author.orcid0000-0001-5988-5868[9]
unesp.author.orcid0000-0001-6836-3084[7]
unesp.author.orcid0000-0002-5791-6170[15]
unesp.author.orcid0000-0002-4774-8775[5]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, São Vicentept

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