Procongopain from Trypanosoma congolense is processed at basic pH: An unusual feature among cathepsin L-like cysteine proteases

Biological Chemistry

Volumn 384, Issue 6, 2003, Pages 921-927

  Serveau, Carole ^a   Boulangé, Alain ^b,c   Lecaille, Fabien ^a   Gauthier, Francis ^a   Authié, Edith ^b,c   Lalmanach, Gilles ^a  

^a UNIVERSITÉ DE TOURS   (France)

^b INSTITUT DE RECHERCHE POUR LE DÉVELOPPEMENT   (France)

^c INTERNATIONAL LIVESTOCK RESEARCH INSTITUTE   (Kenya)

Author keywords

Cathepsin L; Congopain; Cysteine protease; Processing; Trypanosome

Indexed keywords

CONGOPAIN; CYSTEINE PROTEINASE; DEXTRAN SULFATE; ENZYME PRECURSOR; GLYCOSAMINOGLYCAN; PROCONGOPAIN; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BLOOD VESSEL; CATALYSIS; CATTLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME SYNTHESIS; HOST PARASITE INTERACTION; HYPOTHESIS; IONIC STRENGTH; NONHUMAN; PARASITE VIRULENCE; PH; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTOZOAL INFECTION; TRYPANOSOMA CONGOLENSE;

ANIMALS; CATHEPSINS; CATTLE; CYSTEINE ENDOPEPTIDASES; DEXTRAN SULFATE; ENZYME ACTIVATION; ENZYME PRECURSORS; HYDROGEN-ION CONCENTRATION; OSMOLAR CONCENTRATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; TRYPANOSOMA CONGOLENSE;

ANIMALIA; BOS TAURUS; TRYPANOSOMA; TRYPANOSOMA CONGOLENSE;

EID: 0038486742     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.103     Document Type: Article

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