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dc.contributor.authorSaramago, Luizpt_BR
dc.contributor.authorFranceschi, Mariana Ferreira da Silvapt_BR
dc.contributor.authorLogullo, Carlospt_BR
dc.contributor.authorMasuda, Aoipt_BR
dc.contributor.authorVaz Junior, Itabajara da Silvapt_BR
dc.contributor.authorFarias, Sandra Estrazulaspt_BR
dc.contributor.authorMoraes, Jorgept_BR
dc.date.accessioned2023-11-25T03:26:12Zpt_BR
dc.date.issued2012pt_BR
dc.identifier.issn1422-0067pt_BR
dc.identifier.urihttp://hdl.handle.net/10183/267613pt_BR
dc.description.abstractIn the present work, we produced two monoclonal antibodies (BrBm37 and BrBm38) and tested their action against the triosephosphate isomerase of Rhipicephalus (Boophilus) microplus (RmTIM). These antibodies recognize epitopes on both the native and recombinant forms of the protein. rRmTIM inhibition by BrBm37 was up to 85% whereas that of BrBrm38 was 98%, depending on the antibody-enzyme ratio. RmTIM activity was lower in ovarian, gut, and fat body tissue extracts treated with BrBm37 or BrBm38 mAbs. The proliferation of the embryonic tick cell line (BME26) was inhibited by BrBm37 and BrBm38 mAbs. In summary, the results reveal that it is possible to interfere with the RmTIM function using antibodies, even in intact cells.en
dc.format.mimetypeapplication/pdfpt_BR
dc.language.isoengpt_BR
dc.relation.ispartofInternational journal of molecular sciences. Basel. Vol. 13, no. 1 (Jan. 2012), p. 13118-13133pt_BR
dc.rightsOpen Accessen
dc.subjectTriosephosphate isomeraseen
dc.subjectAnticorpos monoclonaispt_BR
dc.subjectGlycolytic pathwayen
dc.subjectBiotecnologia : Animalpt_BR
dc.subjectMonoclonal antibodyen
dc.subjectRiphicephalus (Boophilus) micropluspt_BR
dc.titleInhibition of enzyne activity of Riphicephalus (Boophilus) microplus triosephosphate isomerase and BME26 cell growth by monoclonal antibodiespt_BR
dc.typeArtigo de periódicopt_BR
dc.identifier.nrb000863443pt_BR
dc.type.originEstrangeiropt_BR


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