Hydrolysis of synthetic peptides by cruzipain, the major cysteine proteinase from Trypanosoma cruzi, provides evidence for self-processing and the possibility of more specific substrates for the enzyme.

Cellular and molecular biology (Noisy-le-Grand, France)

Volumn 42, Issue 5, 1996, Pages 691-696

  Cazzulo, J J ^a   Bravo, M ^a   Raimondi, A ^a   Engstrom U ^a   Lindeberg, G ^a   Hellman, U ^a  

^a FUNDACIÓN INSTITUTO LELOIR   (Argentina)

Author keywords

[No Author keywords available]

Indexed keywords

CRUZIPAIN; CYSTEINE PROTEINASE; OLIGOPEPTIDE; PEPTIDE FRAGMENT;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BINDING SITE; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; HYDROLYSIS; KINETICS; METABOLISM; PH; PROTEIN PROCESSING; SYNTHESIS; TRYPANOSOMA CRUZI;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CYSTEINE ENDOPEPTIDASES; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; OLIGOPEPTIDES; PEPTIDE FRAGMENTS; PROTEIN PROCESSING, POST-TRANSLATIONAL; SUBSTRATE SPECIFICITY; TRYPANOSOMA CRUZI;

EID: 0030178647     PISSN: 01455680     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (0)