| Author | Schenkman, Sergio | |
| Author | Chaves, Luciana Botelho | |
| Author | Pontes-de-Carvalho, Lain Carlos | |
| Author | Eichinged, Daniel | |
| Access date | 2017-06-28T14:30:44Z | |
| Available date | 2017-06-28T14:30:44Z | |
| Document date | 1994 | |
| Citation | SCHENKMAN, S. et al. A Proteolytic fragment of Trypanosoma cruzi trans-sialidase lacking the carboxyl-terminal domain is active, monomeric, and generates antibodies that inhibit enzymatic activity. Journal of Biological Chemistry, v. 269, n. 11, p. 7970-7975, 1994. | pt_BR |
| ISSN | 0021-9258 | pt_BR |
| URI | https://www.arca.fiocruz.br/handle/icict/19553 | |
| Description | Pontes-de-Carvalho, Lain Carlos “Documento produzido em parceria ou por autor vinculado à Fiocruz, mas não consta à informação no documento”. | pt_BR |
| Sponsorship | Fundação de Amparo a Pesquisa do Estado de São Paulo, Conselho Nacional de Desenvolvimento
Cientifico e Tecnológico, UNDPMorld BanWWHO Special Program for Research and Training in Tropical Diseases, TheRockefeller Foundation. | pt_BR |
| Language | eng | pt_BR |
| Publisher | American Society for Biochemistry and Molecular Biology | pt_BR |
| Rights | open access | pt_BR |
| Subject in Portuguese | Trypanosoma cruzi | pt_BR |
| Subject in Portuguese | Doença de Chagas | pt_BR |
| Subject in Portuguese | Sialidase | pt_BR |
| Subject in Portuguese | Enzima | pt_BR |
| Subject in Portuguese | Ácido siálico | pt_BR |
| Title | A Proteolytic Fragment of Trypanosoma cruzi trans-Sialidase Lacking the Carboxyl-terminal Domain Is Active, Monomeric, and Generates Antibodies That Inhibit Enzymatic Activity | pt_BR |
| Type | Article | pt_BR |
| Abstract | trans-Sialidase isolated from trypomastigote forms of
IlZypanosoma cruzi, the protozoan parasite that causes
Chagas’ disease, is multimeric and heterogeneous in
size. We show here that limited proteolysis of trans-sialidase
with papain yields a single monomeric polypeptide
chain of 70 kDa that conserves full enzymatic activity on
soluble and membrane-bound substrates. The papain
fragment lacks most otfh e 12-amino acid repeats of the
carboxyl-terminal domain that comprises about 50% of
the native trans-sialidase. When injected into rabbits,
the papain-generated fragmenitn duces antibodies that
inhibit trans-sialidase activity and trypomastigote sialylation.
The repeats are also not required for the stability
of the enzyme or fotrh e correct folding during the
biosynthesis in Escherichia coli, but seem essential for
trans-sialidase oligomerization. We conclude that transsialidase
is composed of two structurally and functionally
independent domains. | pt_BR |
| Affilliation | Escola Paulista de Medicina. Department of Microbiology, Immunology and Parasitology. São Paulo, SP, Brazil | pt_BR |
| Affilliation | Escola Paulista de Medicina. Department of Microbiology, Immunology and Parasitology. São Paulo, SP, Brazil | pt_BR |
| Affilliation | New York University Medical Center. Michael Heidelberger Division of Immunology. New York, New York | pt_BR |
| Affilliation | New York University Medical Center. Michael Heidelberger Division of Immunology. New York, New York | pt_BR |
| Subject | Trypanosoma cruzi | pt_BR |
| Subject | Chagas disease | pt_BR |
| Subject | Sialidase | pt_BR |
| Subject | Enzyme | pt_BR |
| Subject | Sialic acid | pt_BR |
