title: The pyruvate kinase-coupled assay for ATPases: a critical analysis.
abstract: The pyruvate kinase assay for ATPases suffers from major systematic errors due to the variable amounts of the inhibitory product, ADP, present as the rates change. A simple method is presented to estimate the true uninhibited rates and the ADP inhibition constant for the ATPase.
authors.affiliation: Department of Chemistry, Indiana University, Bloomington 47405.
authors.forename: W T
authors.initials: WT
authors.lastname: Jenkins
mesh_terms: D000244:Adenosine Diphosphate / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D008722:Methods; D011770:Pyruvate Kinase / Q000378:metabolism*
chemical_list: D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D007770:L-Lactate Dehydrogenase; D011770:Pyruvate Kinase; D000251:Adenosine Triphosphatases