Anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi in relation to its apparent molecular mass
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 enzy...
Guardado en:
| Autor principal: | |
|---|---|
| Publicado: |
1992
|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781097_v95_n2-3_p225_Martinez http://hdl.handle.net/20.500.12110/paper_03781097_v95_n2-3_p225_Martinez |
| Aporte de: |
| id |
paper:paper_03781097_v95_n2-3_p225_Martinez |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_03781097_v95_n2-3_p225_Martinez2023-06-08T15:39:13Z Anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi in relation to its apparent molecular mass Martinez, Javier Augusto 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 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. Fil:Martínez, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1992 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781097_v95_n2-3_p225_Martinez http://hdl.handle.net/20.500.12110/paper_03781097_v95_n2-3_p225_Martinez |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Martinez, Javier Augusto Anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi in relation to its apparent molecular mass |
| topic_facet |
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 |
| description |
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. |
| author |
Martinez, Javier Augusto |
| author_facet |
Martinez, Javier Augusto |
| author_sort |
Martinez, Javier Augusto |
| title |
Anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi in relation to its apparent molecular mass |
| title_short |
Anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi in relation to its apparent molecular mass |
| title_full |
Anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi in relation to its apparent molecular mass |
| title_fullStr |
Anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi in relation to its apparent molecular mass |
| title_full_unstemmed |
Anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi in relation to its apparent molecular mass |
| title_sort |
anomalous electrophoretic behaviour of the major cysteine proteinase (cruzipain) from trypanosoma cruzi in relation to its apparent molecular mass |
| publishDate |
1992 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781097_v95_n2-3_p225_Martinez http://hdl.handle.net/20.500.12110/paper_03781097_v95_n2-3_p225_Martinez |
| work_keys_str_mv |
AT martinezjavieraugusto anomalouselectrophoreticbehaviourofthemajorcysteineproteinasecruzipainfromtrypanosomacruziinrelationtoitsapparentmolecularmass |
| _version_ |
1768545192258830336 |