Error structure as a function of substrate and inhibitor concentration in enzyme kinetic experiments.
Optimal design of experiments as well as proper analysis of data are dependent on knowledge of the experimental error. A detailed analysis of the error structure of kinetic data obtained with acetylcholinesterase showed conclusively that the classical assumptions of constant absolute or constant relative error are inadequate for the dependent variable (velocity). The best mathematical models for the experimental error involved the substrate and inhibitor concentrations and reflected the rate law for the initial velocity. Data obtained with other enzymes displayed similar relationships between experimental error and the independent variables. The new empirical error functions were shown superior to previously used models when utilized in weighted non-linear-regression analysis of kinetic data. The results suggest that, in the spectrophotometric assays used in the present study, the observed experimental variance is primarily due to errors in determination of the concentrations of substrate and inhibitor and not to error in measuring the velocity.
D000109:Acetylcholine / Q000378:metabolism; D000110:Acetylcholinesterase / Q000378:metabolism; D002800:Cholinesterase Inhibitors / Q000494:pharmacology; D003650:Decamethonium Compounds / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004798:Enzymes / Q000378:metabolism*; D005982:Glutathione Transferase / Q000378:metabolism; D007700:Kinetics; D008956:Models, Chemical
D002800:Cholinesterase Inhibitors; D003650:Decamethonium Compounds; D004791:Enzyme Inhibitors; D004798:Enzymes; C033019:decamethonium; D005982:Glutathione Transferase; D000110:Acetylcholinesterase; D000109:Acetylcholine