Inhibition of cruzipain, the major cysteine proteinase of the protozoan parasite, Trypanosoma cruzi, by proteinase inhibitors of the cystatin superfamily
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 t...
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1995
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v370_n1-2_p101_Stoka http://hdl.handle.net/20.500.12110/paper_00145793_v370_n1-2_p101_Stoka |
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paper:paper_00145793_v370_n1-2_p101_Stoka2023-06-08T14:37:38Z Inhibition of cruzipain, the major cysteine proteinase of the protozoan parasite, Trypanosoma cruzi, by proteinase inhibitors of the cystatin superfamily Labriola, Carlos Alberto Cruzipain Cystatin Cysteine proteinase Inhibition Kinetics Trypanosoma cruzi cruzipain cystatin cystatin c cysteine proteinase kininogen proteinase inhibitor stefin a stefin b article enzyme inhibition enzyme purification enzyme structure ph priority journal trypanosoma cruzi Animal Chickens Comparative Study Cystatins Cysteine Endopeptidases Electrophoresis, Polyacrylamide Gel Human Isoelectric Focusing Kinetics Molecular Weight Recombinant Proteins Support, Non-U.S. Gov't Trypanosoma cruzi 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 (kass = 1.7-79 × 106M-1s-1, Kd = 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. © 1995. Fil:Labriola, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1995 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v370_n1-2_p101_Stoka http://hdl.handle.net/20.500.12110/paper_00145793_v370_n1-2_p101_Stoka |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Cruzipain Cystatin Cysteine proteinase Inhibition Kinetics Trypanosoma cruzi cruzipain cystatin cystatin c cysteine proteinase kininogen proteinase inhibitor stefin a stefin b article enzyme inhibition enzyme purification enzyme structure ph priority journal trypanosoma cruzi Animal Chickens Comparative Study Cystatins Cysteine Endopeptidases Electrophoresis, Polyacrylamide Gel Human Isoelectric Focusing Kinetics Molecular Weight Recombinant Proteins Support, Non-U.S. Gov't Trypanosoma cruzi |
| spellingShingle |
Cruzipain Cystatin Cysteine proteinase Inhibition Kinetics Trypanosoma cruzi cruzipain cystatin cystatin c cysteine proteinase kininogen proteinase inhibitor stefin a stefin b article enzyme inhibition enzyme purification enzyme structure ph priority journal trypanosoma cruzi Animal Chickens Comparative Study Cystatins Cysteine Endopeptidases Electrophoresis, Polyacrylamide Gel Human Isoelectric Focusing Kinetics Molecular Weight Recombinant Proteins Support, Non-U.S. Gov't Trypanosoma cruzi Labriola, Carlos Alberto Inhibition of cruzipain, the major cysteine proteinase of the protozoan parasite, Trypanosoma cruzi, by proteinase inhibitors of the cystatin superfamily |
| topic_facet |
Cruzipain Cystatin Cysteine proteinase Inhibition Kinetics Trypanosoma cruzi cruzipain cystatin cystatin c cysteine proteinase kininogen proteinase inhibitor stefin a stefin b article enzyme inhibition enzyme purification enzyme structure ph priority journal trypanosoma cruzi Animal Chickens Comparative Study Cystatins Cysteine Endopeptidases Electrophoresis, Polyacrylamide Gel Human Isoelectric Focusing Kinetics Molecular Weight Recombinant Proteins Support, Non-U.S. Gov't Trypanosoma cruzi |
| description |
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 (kass = 1.7-79 × 106M-1s-1, Kd = 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. © 1995. |
| author |
Labriola, Carlos Alberto |
| author_facet |
Labriola, Carlos Alberto |
| author_sort |
Labriola, Carlos Alberto |
| title |
Inhibition of cruzipain, the major cysteine proteinase of the protozoan parasite, Trypanosoma cruzi, by proteinase inhibitors of the cystatin superfamily |
| title_short |
Inhibition of cruzipain, the major cysteine proteinase of the protozoan parasite, Trypanosoma cruzi, by proteinase inhibitors of the cystatin superfamily |
| title_full |
Inhibition of cruzipain, the major cysteine proteinase of the protozoan parasite, Trypanosoma cruzi, by proteinase inhibitors of the cystatin superfamily |
| title_fullStr |
Inhibition of cruzipain, the major cysteine proteinase of the protozoan parasite, Trypanosoma cruzi, by proteinase inhibitors of the cystatin superfamily |
| title_full_unstemmed |
Inhibition of cruzipain, the major cysteine proteinase of the protozoan parasite, Trypanosoma cruzi, by proteinase inhibitors of the cystatin superfamily |
| title_sort |
inhibition of cruzipain, the major cysteine proteinase of the protozoan parasite, trypanosoma cruzi, by proteinase inhibitors of the cystatin superfamily |
| publishDate |
1995 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v370_n1-2_p101_Stoka http://hdl.handle.net/20.500.12110/paper_00145793_v370_n1-2_p101_Stoka |
| work_keys_str_mv |
AT labriolacarlosalberto inhibitionofcruzipainthemajorcysteineproteinaseoftheprotozoanparasitetrypanosomacruzibyproteinaseinhibitorsofthecystatinsuperfamily |
| _version_ |
1768545447574503424 |