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Inhibition of cruzipain, the major cysteine proteinase of the protozoan parasite, Trypanosoma cruzi , by proteinase inhibitors of the cystatin superfamily
Author(s) -
Stoka Veronika,
Nycander Maria,
Lenarčič Brigita,
Labriola Carlos,
Cazzulo Juan José,
Björk Ingemar,
Turk Vito
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00798-e
Subject(s) - trypanosoma cruzi , cystatin , cystatin c , cysteine , biochemistry , biology , enzyme , chagas disease , parasite hosting , chemistry , microbiology and biotechnology , virology , renal function , world wide web , computer science
Cruzipain, the major cysteine proteinase from Trypanosoma cruzi epimastigotes, purified to a sequentially pure form, exists in multiple forms with pI values between 3.7 and 5.1, and an apparent molecular mass of 41 kDa. The enzyme is stable between pH 4.5–9.5. Cruzipain was found to be rapidly and tightly inhibited by various protein inhibitors of the cystatin superfamily ( k ass = 1.7–79 × 10 6 M −1 s −1 , K d = 1.4–72 pM). These results suggest a possible defensive role for the host's cystatins after parasite infection, and may be of use for the design of new therapeutic drugs.