Purification and properties of an acid phosphatase from Entamoeba histolytica HM-1:IMSS.
Entamoeba histolytica contains and secretes acid phosphatase, which has been proposed as a virulence factor in some pathogenic microorganisms. In this work, we purified and characterised a membrane-bound acid phosphatase (MAP) from E. histolytica HM-1:IMSS and studied the effect of different chemical compounds on the secreted acid phosphatase and MAP activities. MAP purification was accomplished by detergent solubilisation, and affinity and ion exchange chromatographies. The enzyme showed a pI of 5.5-6.2, an optimum pH of 5.5, and a Km value of 1.14 mM with p-nitrophenyl phosphate.
Aguirre-García
M M
MM
Experimental Pathology Department, Center for Research and Advanced Studies, IPN, México.
Cerbón
J
J
Talamás-Rohana
P
P
D000135:Acid Phosphatase / Q000302:isolation & purification*; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004748:Entamoeba histolytica / Q000201:enzymology*; D007526:Isoelectric Point; D007700:Kinetics; D009596:Nitrophenols / Q000378:metabolism; D009943:Organophosphorus Compounds / Q000378:metabolism; D012995:Solubility
D009596:Nitrophenols; D009943:Organophosphorus Compounds; C008644:nitrophenylphosphate; D000135:Acid Phosphatase