dc.date.accessioned2022-10-25T19:54:10Z
dc.date.accessioned2023-05-23T18:54:08Z
dc.date.available2022-10-25T19:54:10Z
dc.date.available2023-05-23T18:54:08Z
dc.date.created2022-10-25T19:54:10Z
dc.date.issued1989
dc.identifierhttps://hdl.handle.net/20.500.12866/12469
dc.identifierhttps://doi.org/10.1016/0166-6851(89)90146-1
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/6395011
dc.description.abstractAdult Fasciola hepatica worms contain multiple proteinases capable of degrading hemoglobin, immunoglobulins and collagen. Here we report the isolation and biochemical characterization of a cysteine proteinase from acidic extracts of these worms. The enzyme was purified to homogeneity by cation exchange and molecular sieve high-performance liquid chromatography. It eluted at a native molecular weight of approximately 14 500 and migrated as a single band at approximately 14 500 Da upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Activity was assessed by employing synthetic peptide substrates, such as carbobenzoxy-phenylalanyl-arginyl-7-amino-4-trifluoro-methylcoumarin, commonly used to assay other cysteine proteinases. The proteinase was maximally active at pH 6.0, with 50% or more of the activity detected between pH 4.5 and 7.5. Inhibition of activity at pH 5.5 was seen only with compounds known to inhibit cysteine proteinases. No effect was seen with inhibitors of aspartic. serine, or metalloproteinases. The purified enzyme was stable at acidic pH at 4°C, 25°C, -20°C, and in 1 M urea.
dc.languageeng
dc.publisherElsevier
dc.relationMolecular and Biochemical Parasitology
dc.relation1872-9428
dc.rightshttps://creativecommons.org/licenses/by-nc-nd/4.0/deed.es
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectCysteine proteinase
dc.subjectFasciola hepatica
dc.subjectTrematode, parasitic
dc.titleIsolation and characterization of a cysteine proteinase from Fasciola hepatica adult worms
dc.typeinfo:eu-repo/semantics/article


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