Immobilized Cratylia mollis lectin: An affinity matrix to purify a soybean (Glycine max) seed protein with in vitro platelet antiaggregation and anticoagulant activities

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dc.contributor.authorSilva, Mariana C. C. [UNIFESP]
dc.contributor.authorSantana, Lucimeire A. [UNIFESP]
dc.contributor.authorSilva-Lucca, Rosemeire A.
dc.contributor.authorLima, Amanda L. R.
dc.contributor.authorFerreira, Joana G. [UNIFESP]
dc.contributor.authorPaiva, Patricia M. G.
dc.contributor.authorCoelho, Luana C. B. B.
dc.contributor.authorOliva, Maria L. V. [UNIFESP]
dc.contributor.authorZingali, Russolina B.
dc.contributor.authorCorreia, Maria T. S.
dc.contributor.institutionUniversidade Federal de Pernambuco (UFPE)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Estadual Oeste Parana
dc.contributor.institutionUniversidade Federal do Rio de Janeiro (UFRJ)
dc.date.accessioned2016-01-24T14:05:59Z
dc.date.available2016-01-24T14:05:59Z
dc.date.issued2011-01-01
dc.description.abstractLectins, proteins which recognize selectively carbohydrates, have been used as affinity chromatography to purify glycoproteins. Cratylia mollis seed lectin (Cramoll 1,4), of mannose/glucose binding class, immobilized on Sepharose CL-4B, was used as affinity matrix. This paper describes the purification by Cramoll 1,4-Sepharose matrix, and characterization of an anti-platelet and anticoagulant soybean (Glycine max) protein, ApcSP, and its in vitro platelet antiaggregation and anticoagulant activities. SDS-PAGE of ApcSP purified under reducing condition revealed a single glycosilated band of 51 kDa. the N-terminal 10-residue sequence of ApcSP is EGQFGPMIQS, distinct to other soybean seed proteins, such as peroxidase, lectin, 2S albumin and trypsin inhibitor. Deconvolution of CD spectrum indicated 35% alpha-helix, 17% beta-strand, 22% turn and 26% unordered structure; ApcSP fluorescence spectrum showed a maximum emission around 339 nm. the hemostatic parameters revealed inhibition of collagen (p<0.001), thrombin (p<0.05) and ADP (p<0.001)-induced platelet aggregation in the presence of ApcSP (2 mu M), in relation to positive control. the soy protein prolonged the blood coagulation time (activated partial thromboplastin time, more affected, and prothrombin time). the results indicated that immobilized Cramoll 1,4 lectin has the potential to isolate soybean glycoproteins and ApcSP may be important for anti-thrombotic and anticoagulant therapy. (C) 2010 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv Fed Pernambuco, Dept Bioquim, BR-50670420 Recife, PE, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniv Estadual Oeste Parana, Ctr Engn & Ciencias Exatas, BR-85903000 Toledo, PR, Brazil
dc.description.affiliationUniv Fed Rio de Janeiro, Inst Bioquim Med, BR-21941590 Rio de Janeiro, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipFundacao de Amparo a Ciencia e Tecnologia do Estado de Pernambuco (FACEPE)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.format.extent74-80
dc.identifierhttp://dx.doi.org/10.1016/j.procbio.2010.07.017
dc.identifier.citationProcess Biochemistry. Oxford: Elsevier B.V., v. 46, n. 1, p. 74-80, 2011.
dc.identifier.doi10.1016/j.procbio.2010.07.017
dc.identifier.issn1359-5113
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/33287
dc.identifier.wosWOS:000286538300009
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofProcess Biochemistry
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectAntiaggreganten
dc.subjectAnticoagulanten
dc.subjectCramoll 1,4-Sepharoseen
dc.subjectGlycine maxen
dc.subjectGlycoproteinen
dc.subjectLectinen
dc.titleImmobilized Cratylia mollis lectin: An affinity matrix to purify a soybean (Glycine max) seed protein with in vitro platelet antiaggregation and anticoagulant activitiesen
dc.typeinfo:eu-repo/semantics/article
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