Electrophoretic detection of Trypanosoma cruzi peptidases.
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.
Department of Pure and Applied Biology, Imperial College of Science, Technology and Medicine, London, U.K.
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Greig
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Ashall
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D003593:Cytoplasm / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D005780:Gelatin / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000032:analysis*; D011480:Protease Inhibitors / Q000494:pharmacology; D014349:Trypanosoma cruzi / Q000201:enzymology*
D011480:Protease Inhibitors; D005780:Gelatin; D010447:Peptide Hydrolases