Susceptibility to proteolysis of triosephosphate isomerase from two pathogenic parasites: Characterization of an enzyme with an intact and a nicked monomer

Proteins: Structure, Function and Genetics

Volumn 48, Issue 3, 2002, Pages 580-590

  Reyes Vivas, Horacio ^a   Martínez Martínez, Eduardo ^a   Mendoza Hernández, Guillermo ^b   López Velázquez, Gabriel ^c   Pérez Montfort, Ruy ^a   Tuena De Gómez Puyou, Marietta ^a   Gómez Puyou, Armando ^a  

^a INSTITUTO DE FISIOLOGÍA CELULAR   (Mexico)

^b UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^c INSTITUTO NACIONAL DE PEDIATRÍA   (Mexico)

Author keywords

Asymmetrical dimers; Inactivation by limited hydrolysis; Protein structural stability; Structural flexibility; Subtilisin

Indexed keywords

DIMER; GLYCERALDEHYDE 3 PHOSPHATE; MONOMER; SUBTILISIN; TRIOSEPHOSPHATE ISOMERASE;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME DEGRADATION; HYDROLYSIS; MOLECULAR WEIGHT; NONHUMAN; PARASITE; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN STRUCTURE; SPECIES DIFFERENCE; TRYPANOSOMA BRUCEI; TRYPANOSOMA CRUZI;

AMINO ACID SEQUENCE; ANIMALS; ELECTROPHORESIS; ENZYME STABILITY; HYDROLYSIS; KINETICS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; SEQUENCE ALIGNMENT; SUBTILISIN; TRIOSE-PHOSPHATE ISOMERASE; TRYPANOSOMA BRUCEI BRUCEI; TRYPANOSOMA CRUZI;

TRYPANOSOMA; TRYPANOSOMA BRUCEI; TRYPANOSOMA CRUZI;

EID: 0037103071     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10179     Document Type: Article

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