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Secretory Hydrolases of Entamoeba histolytica 1
Author(s) -
MÜLLER FRIEDRICHWILHELM,
FRANZ ALFRED,
WERRIES ECKHARD
Publication year - 1988
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.1550-7408.1988.tb04346.x
Subject(s) - entamoeba histolytica , sephadex , acid phosphatase , enzyme , esterase , extracellular , biochemistry , biology , alcohol dehydrogenase , lactate dehydrogenase , dehydrogenase , size exclusion chromatography , parasite hosting , chemistry , microbiology and biotechnology , world wide web , computer science
Cells of Entamoeba histolytica grown over a period of four days contained NADP + ‐dependent alcohol dehydrogenase exclusively inside the cells. No activity of this enzyme could be found in the growth medium after harvesting the cells. Under the same conditions, acid phosphatase, β‐N‐acetylglucosaminidase, esterase, α‐glucosidase, and different amylases of the parasite were found both inside the cells and in the medium. The activities present in the cell homogenate and in the medium before and after growth of the amoebas were partially separated by gel filtration on Sephadex G150 and G75, respectively. The comparison of the elution diagrams revealed that NADP + ‐dependent alcohol dehydrogenase, acid phosphatase, esterase, and amylases occurred as multiple forms inside the cells. These activities, as well as β‐N‐acetylglucosaminidase and α‐glucosidase, were released into the extracellular environment to a different degree. The enzymes originating from the parasite were identified and distinguished from those of the ingredients of the growth medium according to their molecular mass and pH optimum. Furthermore, the amoebic origin of the secreted enzymes was shown on the basis of their inhibition by antibodies prepared against the supernatant fraction of the homogenate.