title: Specific features of phosphomonoesterase of Entamoeba histolytica (NIH-200).
abstract: Axenically grown E. histolytica possess significant acid phosphatase activity. The Km of the enzyme was found to be 7.1 x 10(-3) and was maximally active at pH 4.5. Acid phosphatase activity was significantly inhibited by Cu2+, cysteine and was activated by tartrate and fluoride. It was found that E. histolytica acid phosphatase differs in some properties as compared to the enzyme reported from other sources.
authors.affiliation: Division of Biochemistry, Central Drug Research Institute, Lucknow, India.
authors.forename: A
authors.initials: A
authors.lastname: Agrawal
authors.forename: H C
authors.initials: HC
authors.lastname: Prasad
authors.forename: V C
authors.initials: VC
authors.lastname: Pandey
authors.forename: P
authors.initials: P
authors.lastname: Sagar
mesh_terms: D000818:Animals; D003300:Copper / Q000494:pharmacology; D003545:Cysteine / Q000494:pharmacology; D004748:Entamoeba histolytica / Q000201:enzymology*; D004789:Enzyme Activation; D005459:Fluorides / Q000494:pharmacology; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013644:Tartrates / Q000494:pharmacology
chemical_list: D013644:Tartrates; D003300:Copper; D010744:Phosphoric Monoester Hydrolases; D003545:Cysteine; D005459:Fluorides