Sulfhydryl reagent susceptibility in proteins with high sequence similarity: Triosephosphate isomerase from Trypanosoma brucei, Trypanosoma cruzi and Leishmania mexicana

European Journal of Biochemistry

Volumn 253, Issue 3, 1998, Pages 684-691

  Garza Ramos, Georgina ^a,b   Cabrera, Nallely ^a   Saavedra Lira, Emma ^a   Tuena De Gómez Puyou, Marietta ^b   Ostoa Saloma, Pedro ^a   Pérez Montfort, Ruy ^a   Gómez Puyou, Armando ^a  

^a UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^b INSTITUTO DE FISIOLOGÍA CELULAR   (Mexico)

Author keywords

Cysteine residue; Protein changes; Protein conformations; Triosephosphate isomerase; Trypanosome

Indexed keywords

CYSTEINE; THIOL REAGENT; TRIOSEPHOSPHATE ISOMERASE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME CONFORMATION; ENZYME PURIFICATION; ENZYME STABILITY; LEISHMANIA MEXICANA; NONHUMAN; PH; PRIORITY JOURNAL; TRYPANOSOMA BRUCEI; TRYPANOSOMA CRUZI;

ANIMALS; CYSTEINE; DITHIONITROBENZOIC ACID; KINETICS; LEISHMANIA MEXICANA; METHYL METHANESULFONATE; MUTAGENESIS, SITE-DIRECTED; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SULFHYDRYL REAGENTS; TRIOSE-PHOSPHATE ISOMERASE; TRYPANOSOMA BRUCEI BRUCEI; TRYPANOSOMA CRUZI;

LEISHMANIA MEXICANA; TRYPANOSOMA; TRYPANOSOMA BRUCEI; TRYPANOSOMA CRUZI;

EID: 0032079362     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2530684.x     Document Type: Article

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