Artículo
Cazzulo, J.J.; Martínez, J.; Parodi, A.J.A.; Wernstedt, C.; Hellman, U. "On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi" (1992) FEMS Microbiology Letters. 100(1-3):411-416
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Abstract:
Cruzipain, the major cysteine proteinase from Trypanosoma cruzi, has a 130 amino acid-long C-terminal domain, which, although microheterogeneous in SDS-PAGE, has a single N-terminal amino acid sequence. Most of the Thr residues present at the beginning of this sequence are modified; the nature of this modification is still unknown, but O-glycosylation and phosphorylation seem both to be absent. The only potential site for N-glycosylation (Asn 254) is glycosylated in vivo. Most of the eight Cys residues are involved in disulfide bridges. The results are consistent with cruzipain being made of two well-defined domains, a catalytic one with high homology to cathepsin L, and a C-terminal domain, linked to the former by a 'hinge' corresponding to the Pro-and Thr-rich region at its N-terminus. © 1992.
Registro:
| Documento: | Artículo |
| Título: | On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi |
| Autor: | Cazzulo, J.J.; Martínez, J.; Parodi, A.J.A.; Wernstedt, C.; Hellman, U. |
| Filiación: | Instituto de Investigaciones Bioquímicas 'Luis F. Leloir', Fundación Campomar-CONICET-Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina, USA Ludwig Institute for Cancer Research, Uppsala Branch, Uppsala, Sweden |
| Palabras clave: | Cruzipain; Cysteine proteinase; Posttranslational modification; Proteinase; Trypanosoma cruzi; cruzipain; cysteine proteinase; proteinase; cruzipain; cysteine proteinase; peptide fragment; article; nonhuman; priority journal; protein processing; trypanosoma cruzi; amino acid sequence; animal; genetics; isolation and purification; metabolism; molecular genetics; protein processing; Trypanosoma cruzi; Amino Acid Sequence; Animal; Cysteine Endopeptidases; Molecular Sequence Data; Peptide Fragments; Protein Processing, Post-Translational; Support, Non-U.S. Gov't; Trypanosoma cruzi |
| Año: | 1992 |
| Volumen: | 100 |
| Número: | 1-3 |
| Página de inicio: | 411 |
| Página de fin: | 416 |
| DOI: | http://dx.doi.org/10.1016/0378-1097(92)90239-K |
| Título revista: | FEMS Microbiology Letters |
| Título revista abreviado: | FEMS Microbiol. Lett. |
| ISSN: | 03781097 |
| CODEN: | FMLED |
| CAS: | cysteine proteinase, 37353-41-6; proteinase, 9001-92-7; cruzipain, EC 3.4.22.-; Cysteine Endopeptidases, EC 3.4.22; Peptide Fragments |
| Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781097_v100_n1-3_p411_Cazzulo |
Referencias:
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Citas:
---------- APA ----------
Cazzulo, J.J., Martínez, J., Parodi, A.J.A., Wernstedt, C. & Hellman, U. (1992) . On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi. FEMS Microbiology Letters, 100(1-3), 411-416.http://dx.doi.org/10.1016/0378-1097(92)90239-K
---------- CHICAGO ----------
Cazzulo, J.J., Martínez, J., Parodi, A.J.A., Wernstedt, C., Hellman, U. "On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi" . FEMS Microbiology Letters 100, no. 1-3 (1992) : 411-416.http://dx.doi.org/10.1016/0378-1097(92)90239-K
---------- MLA ----------
Cazzulo, J.J., Martínez, J., Parodi, A.J.A., Wernstedt, C., Hellman, U. "On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi" . FEMS Microbiology Letters, vol. 100, no. 1-3, 1992, pp. 411-416.http://dx.doi.org/10.1016/0378-1097(92)90239-K
---------- VANCOUVER ----------
Cazzulo, J.J., Martínez, J., Parodi, A.J.A., Wernstedt, C., Hellman, U. On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi. FEMS Microbiol. Lett. 1992;100(1-3):411-416.http://dx.doi.org/10.1016/0378-1097(92)90239-K
