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Secretion of Acid Phosphatase by x4xenic Entamoeba histolytica NIH‐200 and Properties of the Extracellular Enzyme
Author(s) -
AGRAWAL ANJU,
PANDEY V. C.,
KUMAR S.,
SAGAR P.
Publication year - 1989
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.1550-7408.1989.tb02716.x
Subject(s) - entamoeba histolytica , acid phosphatase , enzyme , biochemistry , chemistry , polyacrylamide gel electrophoresis , enzyme assay , concanavalin a , ammonium chloride , ammonium , extracellular , chromatography , biology , microbiology and biotechnology , organic chemistry , in vitro
Entamoeba histolytica (NIH‐200) secreted large amounts of acid phosphatase in its external environment when grown axenically in modified TPS‐II medium. Fractionation by DEAE‐cellulose chromatography of the precipitate obtained from the cell‐free medium at 60% ammonium sulfate saturation yielded 3 distinct peaks of enzyme activity. The enzyme in all the peaks showed resistance to tartrate but was inhibited by fluoride, cupnc chloride, ethylene diamine‐tetra acetic acid, ammonium molybdale and cysteine: however, enzyme associated with different peaks differed in its polyacrylamide gel electrophoretic profiles and behavior towards concanavalin A.