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Acid and Neutral Hydrolases in Trypanosoma cruzi . Characterization and Assay *
Author(s) -
AVILA JOSE LUIS,
CASANOVA MARIA ARGELIA,
AVILA ANGELA,
BRETANA ANTONIO
Publication year - 1979
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1979.tb02786.x
Subject(s) - chemistry , biochemistry , trypanosoma cruzi , acid phosphatase , cathepsin d , enzyme , alpha glucosidase , trehalase , microbiology and biotechnology , beta (programming language) , chromatography , biology , programming language , parasite hosting , world wide web , computer science
SYNOPSIS Twelve acid hydrolases, 4 near‐neutral hydrolases and alkaline phosphatase were demonstrated in 0.34 M sucrose homogenates of Trypanosoma cruzi strain Y: p ‐nitrophenylphosphatase and α‐naphthylphosphatase, with optimum pH at ˜ 6.0; α‐galactosidase, β‐galactosidase, β‐glucosidase, N‐acetyl‐β‐glucosaminidase, cathepsin A and peptidase I and III, with optimum pH between 5.0 and 6.0: and arylsulfatase cathepsin D, α‐arabinase and α‐mannosidase with optimum pH at ˜ 4.0 α‐Glucosidase, gluccse‐6‐phosphatase and peptidase II had optimum pH at ˜ 7.0. β‐Glycerophcsphatase had a broad pH‐activity curve from 4.0 to 7.4, with maximum activity at pH 7.0. The main kinetic characteristics of these enzymes and their quantitative assay methods were studied. No activity was detected for α‐fucosidase, β‐xylosidase, β‐glucuronidase, elaidate esterase. acid lipase, and alkaline phospho‐diesterase.