Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes

Detalhes bibliográficos
Autor(a) principal: Schenkman, Sergio
Data de Publicação: 1992
Outros Autores: Pontes-de-Carvalho, Lain Carlos, Nussenzweig, Victor
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da FIOCRUZ (ARCA)
Texto Completo: https://www.arca.fiocruz.br/handle/icict/19476
Resumo: Pontes-de-Carvalho, L. C. “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”.
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spelling Schenkman, SergioPontes-de-Carvalho, Lain CarlosNussenzweig, Victor2017-06-21T18:15:24Z2017-06-21T18:15:24Z1992SCHENKMAN, S.; PONTES-DE-CARVALHO, L. C.; NUSSENZWEIG, V. Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes. Journal of Experimental Medicine, v. 175, p. 567-575, 1992.0022-1007https://www.arca.fiocruz.br/handle/icict/19476Pontes-de-Carvalho, L. C. “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”.MacArthur Foundation, the UNDP/World Bank/WHO Special Program for Research and Training in Tropical Diseases, Conselho Nacional de Desenvolvimento Científico e Tecnologico, Secretaria de Ciencia e Tecnologia (programa RHAE), and Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (Brazil).Escola Paulista de Medicina. São Paulo, SP, BrasilNew York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New YorkNew York University Medical Center. Department of Pathology and Kaplan Cancer Center. New York, New YorkTrans-sialidase and neuraminidase activities have been detected on the surface membrane of trypomastigotes of Trypanosoma cruzi, and both have been implicated in the parasite's invasion of host cells. We show here that these enzymes are structurally related. They are recognized by two independently derived monoclonal antibodies, are anchored to the membrane by glycosylphosphatidylinositol, copurify by ion exchange, molecular sieving, and hydrophobic chromatography, have maximal activities between pH 6.5 and 7.5, and are inactivated by heating at 56~ Furthermore, the neuraminidase and trans-sialidase reactions are coupled. An increase of the concentration of acceptors of the transfer reaction decreases the amount of flee sialic acid released through the neuraminidase reaction. We conclude that a single enzyme can catalyze the transfer or the hydrolysis of macromolecular-bound sialic acid. The predominant direction of the reaction will depend on the availability of appropriate oligosaccharide acceptors of sialic acid.engRockefeller University PressTrypanosoma cruziEnzimasÁcido siálicoHidróliseTrypanosoma cruziEnzymesSialic acidHydrolysisTrypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da FIOCRUZ (ARCA)instname:Fundação Oswaldo Cruz (FIOCRUZ)instacron:FIOCRUZLICENSElicense.txtlicense.txttext/plain; charset=utf-82991https://www.arca.fiocruz.br/bitstream/icict/19476/1/license.txt5a560609d32a3863062d77ff32785d58MD51ORIGINALSchenkman S Trypanosoma cruzi trans-sialidase....pdfSchenkman S Trypanosoma cruzi 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dc.title.pt_BR.fl_str_mv Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes
title Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes
spellingShingle Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes
Schenkman, Sergio
Trypanosoma cruzi
Enzimas
Ácido siálico
Hidrólise
Trypanosoma cruzi
Enzymes
Sialic acid
Hydrolysis
title_short Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes
title_full Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes
title_fullStr Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes
title_full_unstemmed Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes
title_sort Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes
author Schenkman, Sergio
author_facet Schenkman, Sergio
Pontes-de-Carvalho, Lain Carlos
Nussenzweig, Victor
author_role author
author2 Pontes-de-Carvalho, Lain Carlos
Nussenzweig, Victor
author2_role author
author
dc.contributor.author.fl_str_mv Schenkman, Sergio
Pontes-de-Carvalho, Lain Carlos
Nussenzweig, Victor
dc.subject.other.pt_BR.fl_str_mv Trypanosoma cruzi
Enzimas
Ácido siálico
Hidrólise
topic Trypanosoma cruzi
Enzimas
Ácido siálico
Hidrólise
Trypanosoma cruzi
Enzymes
Sialic acid
Hydrolysis
dc.subject.en.pt_BR.fl_str_mv Trypanosoma cruzi
Enzymes
Sialic acid
Hydrolysis
description Pontes-de-Carvalho, L. C. “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”.
publishDate 1992
dc.date.issued.fl_str_mv 1992
dc.date.accessioned.fl_str_mv 2017-06-21T18:15:24Z
dc.date.available.fl_str_mv 2017-06-21T18:15:24Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.citation.fl_str_mv SCHENKMAN, S.; PONTES-DE-CARVALHO, L. C.; NUSSENZWEIG, V. Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes. Journal of Experimental Medicine, v. 175, p. 567-575, 1992.
dc.identifier.uri.fl_str_mv https://www.arca.fiocruz.br/handle/icict/19476
dc.identifier.issn.pt_BR.fl_str_mv 0022-1007
identifier_str_mv SCHENKMAN, S.; PONTES-DE-CARVALHO, L. C.; NUSSENZWEIG, V. Trypanosoma cruzi Trans-sialidase and Neuraminidase Activities Can Be Mediated by the Same Enzymes. Journal of Experimental Medicine, v. 175, p. 567-575, 1992.
0022-1007
url https://www.arca.fiocruz.br/handle/icict/19476
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dc.publisher.none.fl_str_mv Rockefeller University Press
publisher.none.fl_str_mv Rockefeller University Press
dc.source.none.fl_str_mv reponame:Repositório Institucional da FIOCRUZ (ARCA)
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