TRANS-SIALIDASE FROM TRYPANOSOMA-CRUZI EPIMASTIGOTES IS EXPRESSED AT the STATIONARY-PHASE and IS DIFFERENT FROM the ENZYME EXPRESSED in TRYPOMASTIGOTES

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dc.contributor.authorChaves, L. B.
dc.contributor.authorBriones, MRS
dc.contributor.authorSchenkman, S.
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T11:40:14Z
dc.date.available2016-01-24T11:40:14Z
dc.date.issued1993-09-01
dc.description.abstractWe have studied the trans-sialidase from insect forms of Trypanosoma cruzi growing in axenic culture. Log phase epimastigotes expressed little or-no trans-sialidase activity, and were unable to incorporate exogenous sialic acid. Trans-sialidase started to be expressed at the late logarithmic phase, with specific activity increasing steadily as the culture reached the stationary phase. Trans-sialidase was purified from the late log phase epimastigote culture, which contained less than 2% of metacyclic forms, yielding a glycoprotein that migrated as a single 90-kDa band in sodium dodecyl sulfate gels. This enzyme features: (1) no reaction with antibodies against the peptide repeats present in the carboxy-terminal of trypomastigote trans-sialidase; (2) positive reaction with antibodies raised against a fragment of trypomastigote trans-sialidase that contains the active site; (3) similar kinetic properties and identical acceptor-donor specificity when compared to the trypomastigote enzyme; and (4) neuraminidase activity in the absence of acceptors. Upon differentiation into metacyclic forms, a trans-sialidase activity containing the carboxy-terminal repeats of the trypomastigote enzyme was released into the medium. These results suggest that epimastigotes express a developmentally regulated trans-sialidase that contains the same catalytic site but lacks the tandem amino acid repeats typical of trypomastigote trans-sialidase.en
dc.description.affiliationESCOLA PAULISTA MED,DEPT MICROBIOL IMMUNOL & PARASITOL,RUA BOTUCATU 862-8 ANDAR,BR-04023 São Paulo,BRAZIL
dc.description.affiliationUnifespESCOLA PAULISTA MED,DEPT MICROBIOL IMMUNOL & PARASITOL,RUA BOTUCATU 862-8 ANDAR,BR-04023 São Paulo,BRAZIL
dc.description.sourceWeb of Science
dc.format.extent97-106
dc.identifierhttp://dx.doi.org/10.1016/0166-6851(93)90162-Q
dc.identifier.citationMolecular and Biochemical Parasitology. Amsterdam: Elsevier B.V., v. 61, n. 1, p. 97-106, 1993.
dc.identifier.doi10.1016/0166-6851(93)90162-Q
dc.identifier.issn0166-6851
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/25352
dc.identifier.wosWOS:A1993LZ79600010
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofMolecular and Biochemical Parasitology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectTRYPANOSOMA-CRUZIen
dc.subjectTRANS-SIALIDASEen
dc.subjectSIALIC ACIDen
dc.subjectPURIFICATIONen
dc.subjectANTIGENIC SITEen
dc.titleTRANS-SIALIDASE FROM TRYPANOSOMA-CRUZI EPIMASTIGOTES IS EXPRESSED AT the STATIONARY-PHASE and IS DIFFERENT FROM the ENZYME EXPRESSED in TRYPOMASTIGOTESen
dc.typeinfo:eu-repo/semantics/article
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