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FEBS Letters

Volumn 469, Issue 1, 2000, Pages 29-32

The high stability of cruzipain against pH-induced inactivation is not dependent on its C-terminal domain

(6) Stoka, Veronika a Turk, Boris a McKerrow, James H b Björk, Ingemar c Cazzulo, Juan José d Turk, Vito a

a JO EF STEFAN INSTITUTE (Slovenia)

b UNIVERSITY OF CALIFORNIA (United States)

c SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES (Sweden)

d INSTITUTO DE INVESTIGACIONES BIOTECNOLÓGICAS (Argentina)

Author keywords

Cathepsin; Cruzipain; Lysosomal cysteine protease; pH stability; Trypanosoma cruzi

Indexed keywords

CATHEPSIN; CRUZIPAIN; CYSTEINE PROTEINASE;

ANIMAL EXPERIMENT; ARTICLE; CIRCULAR DICHROISM; ENZYME INACTIVATION; ENZYME STABILITY; ENZYME STRUCTURE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; TRYPANOSOMA CRUZI;

ANIMALS; BINDING SITES; CIRCULAR DICHROISM; CYSTEINE ENDOPEPTIDASES; ELECTROSTATICS; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; KINETICS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; TRYPANOSOMA CRUZI;

MAMMALIA; TRYPANOSOMA; TRYPANOSOMA CRUZI;

EID: 0034598986 PISSN: 00145793 EISSN: None Source Type: Journal
DOI: 10.1016/S0014-5793(00)01221-7 Document Type: Article

Times cited : (10)

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