Secretion of acid phosphatase by axenic Entamoeba histolytica NIH-200 and properties of the extracellular enzyme.
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, cupric chloride, ethylene diamine-tetra acetic acid, ammonium molybdate and cysteine; however, enzyme associated with different peaks differed in its polyacrylamide gel electrophoretic profiles and behavior towards concanavalin A.
Agrawal
A
A
Department of Biochemistry, Central Drug Research Institute, Lucknow, India.
Pandey
V C
VC
Kumar
S
S
Sagar
P
P
D000135:Acid Phosphatase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D003208:Concanavalin A / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004748:Entamoeba histolytica / Q000201:enzymology*; D005856:Germ-Free Life
D003208:Concanavalin A; D000135:Acid Phosphatase