Electrophoretic detection of Trypanosoma cruzi peptides
| Autor: | Frank Ashall, Stephen Greig |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Cytoplasm
Metallopeptidase Trypanosoma cruzi E-64 Biology chemistry.chemical_compound parasitic diseases Animals Protease Inhibitors Molecular Biology Polyacrylamide gel electrophoresis Pathogen chemistry.chemical_classification Gel electrophoresis Hydrolysis Cell Membrane Hydrogen-Ion Concentration biology.organism_classification Molecular biology Molecular Weight Enzyme chemistry Biochemistry Gelatin Protozoa Electrophoresis Polyacrylamide Gel Parasitology Peptide Hydrolases |
| Zdroj: | Molecular and Biochemical Parasitology. 39:31-37 |
| ISSN: | 0166-6851 |
| Popis: | Peptidases of Trypanosoma cruzi epimastigotes were examined by polyacrylamide gel electrophoresis in gels containing gelatin as peptidase substrate. Mini-gels were far superior to large gels in their sensitivity of peptidase detection. Patterns of peptidases were similar between different strains of T. cruzi, although some inter-strain heterogeneity was found. In strain Y, at least five peptidases were detected: four of these enzymes were shown to be cysteine-type peptidases with acidic pH optima. The other peptidase was a 60-kDa membrane-associated peptidase that was sensitive to o-phenanthroline; it was tentatively characterised as a metallopeptidase, and was optimally active at alkaline pH. This membrane-associated peptidase was conserved between strains of T. cruzi. |
| Databáze: | OpenAIRE |
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