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Volumn 268, Issue 24, 2001, Pages 6578-6586
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Comparison of the specificity, stability and individual rate constants with respective activation parameters for the peptidase activity of cruzipain and its recombinant form, cruzain, from trypanosoma cruzi
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Author keywords
C terminal domain; Cruzain; Cruzipain; Cysteine proteinase; Substrate specificity.
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Indexed keywords
ASPARTIC ACID;
CRUZIPAIN;
CYSTEINE;
MANNOSE;
PEPTIDASE;
PEPTIDE DERIVATIVE;
PROTEINASE;
RECOMBINANT ENZYME;
SODIUM CHLORIDE;
ACYLATION;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
COMPARATIVE STUDY;
CONTROLLED STUDY;
DEACYLATION;
DIFFUSION;
DISSOCIATION;
ENERGY;
ENTROPY;
ENZYME ACTIVATION;
ENZYME ACTIVITY;
ENZYME DENATURATION;
ENZYME GLYCOSYLATION;
ENZYME KINETICS;
ENZYME SPECIFICITY;
ENZYME STABILITY;
ENZYME SUBSTRATE;
HYDROLYSIS;
MICHAELIS CONSTANT;
NONHUMAN;
PH;
PRIORITY JOURNAL;
TEMPERATURE DEPENDENCE;
TRYPANOSOMA CRUZI;
AMINO ACID SEQUENCE;
ANIMALS;
CYSTEINE ENDOPEPTIDASES;
ENZYME ACTIVATION;
ENZYME STABILITY;
HEAT;
HYDROGEN-ION CONCENTRATION;
HYDROLYSIS;
KINETICS;
OLIGOPEPTIDES;
PROTEIN DENATURATION;
PROTOZOAN PROTEINS;
RECOMBINANT PROTEINS;
SODIUM CHLORIDE;
SUBSTRATE SPECIFICITY;
TRYPANOSOMA CRUZI;
PROTOZOA;
TRYPANOSOMA;
TRYPANOSOMA CRUZI;
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EID: 0035660408
PISSN: 00142956
EISSN: None
Source Type: Journal
DOI: 10.1046/j.0014-2956.2001.02612.x Document Type: Article |
Times cited : (34)
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References (34)
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