Proteolytic activites in cell extracts of Trypanosoma cruzi.
Cell extracts of culture forms of Trypanosoma cruzi are capable of hydrolysing substances belonging to 4 different groups of protease substrates: (a) substrates for trypsin-like enzymes: benzoyl-arginine-p-nitroanilide and benzoylarginine-naphtylamide; (b) substrates for aminopeptidases: leucyl, lysl and glutamyl-beta-naphtylamide; (c) a substrate fochymotrypsin-like enzymes: carbobenzoxy-L-tyrosine-p-nitorphenylester, and (d) a nonspecific substrate for a broad range of proteases: azocasein. Some physico-chemical characteristics of each enzymic reaction were studied. They were found to be distint enought to allow attributing each hydrolytic activity to a separate enzyme.
D000626:Aminopeptidases / Q000302:isolation & purification / Q000378:metabolism; D000818:Animals; D002364:Caseins; D002918:Chymotrypsin / Q000302:isolation & purification / Q000378:metabolism; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D014349:Trypanosoma cruzi / Q000201:enzymology*
D002364:Caseins; D010447:Peptide Hydrolases; D000626:Aminopeptidases; D002918:Chymotrypsin