TRYPANOSOMA-CRUZI TRANS-SIALIDASE and NEURAMINIDASE ACTIVITIES CAN BE MEDIATED BY the SAME ENZYMES

TRYPANOSOMA-CRUZI TRANS-SIALIDASE and NEURAMINIDASE ACTIVITIES CAN BE MEDIATED BY the SAME ENZYMES

Autor Schenkman, Sergio Autor UNIFESP Google Scholar
Decarvalho, L. P. Google Scholar
Nussenzweig, V. Google Scholar
Instituição NYU MED CTR
Universidade Federal de São Paulo (UNIFESP)
Resumo Trans-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-degrees-C. Furthermore, the neuraminidase and trans-sialidase reactions are coupled. An increase of the concentration of acceptors of the transfer reaction decreases the amount of free 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.
Idioma Inglês
Data de publicação 1992-02-01
Publicado em Journal of Experimental Medicine. New York: Rockefeller Univ Press, v. 175, n. 2, p. 567-575, 1992.
ISSN 0022-1007 (Sherpa/Romeo, fator de impacto)
Publicador Rockefeller Univ Press
Extensão 567-575
Fonte http://dx.doi.org/10.1084/jem.175.2.567
Direito de acesso Acesso aberto Open Access
Tipo Artigo
Web of Science WOS:A1992HB06100028
Endereço permanente http://repositorio.unifesp.br/handle/11600/25240

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