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Abstract:

The molecular mass of cruzipain, the major cysteine proteinase from Trypanosoma cruzi epimastigotes, is 36.3 kDa as calculated from its sequence; this value can increase to about 41 kDa if the three potential N-glycosylation sites are glycosylated in vivo. Yet the apparent molecular mass of the enzyme, as determined by SDS-polyacrylamide gel electrophoresis, has been reported in a range of values from 60 to 40 kDa. We show that the purified enzyme had apparent molecular masses ranging from 51 to 33 kDa, depending on the experimental conditions. This variation is likely to be due to both N-glycosylation and the presence of several disulfide bridges, which make electrophoretic mobility dependent on acrylamide concentration, and reduction and/or boiling of the sample. © 1992.

Registro:

Documento: Artículo
Título:Anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi in relation to its apparent molecular mass
Autor:Martínez, J.; Cazzulo, J.J.
Filiación:Instituto de Investigaciones Bioquímicas 'Luis F. Leloir', Fundación Campomar-Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Palabras clave:Cruzipain; Trypanosoma cruzi; cruzipain; cysteine proteinase; cysteine proteinase; article; molecular weight; nonhuman; priority journal; protein electrophoresis; trypanosoma cruzi; animal; chemistry; enzymology; polyacrylamide gel electrophoresis; Trypanosoma cruzi; Animal; Cysteine Endopeptidases; Electrophoresis, Polyacrylamide Gel; Molecular Weight; Support, Non-U.S. Gov't; Trypanosoma cruzi
Año:1992
Volumen:95
Número:2-3
Página de inicio:225
Página de fin:229
DOI: http://dx.doi.org/10.1016/0378-1097(92)90433-O
Título revista:FEMS Microbiology Letters
Título revista abreviado:FEMS Microbiol. Lett.
ISSN:03781097
CODEN:FMLED
CAS:cysteine proteinase, 37353-41-6; cruzipain, EC 3.4.22.-; Cysteine Endopeptidases, EC 3.4.22
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781097_v95_n2-3_p225_Martinez

Referencias:

  • Cazzulo, (1991) Biochem. Protozool., pp. 191-199. , G.H. Coombs, M.J. North, Taylor & Francis
  • Campetella, Henriksson, Åslund, Frasch, Pettersson, Cazzulo, (1992) Mol. Biochem. Parasitol., 50, pp. 225-234
  • Åslund, Henriksson, Campetella, Frasch, Pettersson, Cazzulo, (1991) Mol. Biochem. Parasitol., 45, pp. 345-348
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  • Campetella, Martinez, Cazzulo, (1990) FEMS Microbiol. Lett., 67, pp. 145-150
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  • Glazer, Smith, (1971) The Enzymes, 3, pp. 501-546. , P.D. Boyer, Academic Press, New York

Citas:

---------- APA ----------
Martínez, J. & Cazzulo, J.J. (1992) . Anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi in relation to its apparent molecular mass. FEMS Microbiology Letters, 95(2-3), 225-229.
http://dx.doi.org/10.1016/0378-1097(92)90433-O
---------- CHICAGO ----------
Martínez, J., Cazzulo, J.J. "Anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi in relation to its apparent molecular mass" . FEMS Microbiology Letters 95, no. 2-3 (1992) : 225-229.
http://dx.doi.org/10.1016/0378-1097(92)90433-O
---------- MLA ----------
Martínez, J., Cazzulo, J.J. "Anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi in relation to its apparent molecular mass" . FEMS Microbiology Letters, vol. 95, no. 2-3, 1992, pp. 225-229.
http://dx.doi.org/10.1016/0378-1097(92)90433-O
---------- VANCOUVER ----------
Martínez, J., Cazzulo, J.J. Anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi in relation to its apparent molecular mass. FEMS Microbiol. Lett. 1992;95(2-3):225-229.
http://dx.doi.org/10.1016/0378-1097(92)90433-O