title: Antimony-Phosphomolybdate ATPase Assay.
abstract: Hydrolytic activity is an important functional parameter of enzymes like adenosinetriphosphatases (ATPases). It is measured to test enzyme functionality, but it also provides useful information on possible inhibitory effects of molecules that interfere with the hydrolytic process. Here, we describe a molybdenum-based protocol that makes use of potassium antimony (III) oxide tartrate and may be valuable in biochemical and biomedical investigations of ATPase enzymes as well as in high-throughput drug screening. This method has been successfully applied to native and recombinant ATPases.
authors.affiliation: Department of Chemistry "Ugo Schiff", University of Florence, Sesto Fiorentino, Italy. gianluca.bartolommei@unifi.it.
authors.forename: Gianluca
authors.initials: G
authors.lastname: Bartolommei
authors.affiliation: Department of Chemistry "Ugo Schiff", University of Florence, Sesto Fiorentino, Italy.
authors.forename: Francesco
authors.initials: F
authors.lastname: Tadini-Buoninsegni
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism; D000966:Antimony Potassium Tartrate / Q000737:chemistry; D004353:Drug Evaluation, Preclinical / Q000379:methods*; D057166:High-Throughput Screening Assays / Q000379:methods*; D006801:Humans; D006868:Hydrolysis; D008982:Molybdenum / Q000737:chemistry
chemical_list: D008982:Molybdenum; D000966:Antimony Potassium Tartrate; D000251:Adenosine Triphosphatases
keywords: ATPases; Antimony-phosphomolybdate; Calibration curve; Colorimetric assay; Enzymes; Hydrolytic activity; Molybdenum blue; UV/Vis spectrophotometry