Related Experiment Video
Updated: Jul 16, 2026

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
Published on: December 19, 2011
Detection of errors of interpretation in experiments in enzyme kinetics
1Institut Fédératif "Biologie Structurale et Microbiologie," Bioénergétique et Ingénierie des Protéines, Centre National de la Recherche Scientifique, 31 chemin Joseph-Aiguier, Marseille Cedex 20, 13402, France. athel@ibsm.cnrs-mrs.fr
Abstract:
Although modern statistical computing will often be the method of choice for analyzing kinetic data, graphic methods provide an important supplement that ought not to be neglected. Residual plots, or plots of differences between observed and calculated values against variables not expected to be correlated with these differences, permit a rapid judgment of whether data have been correctly interpreted and analyzed. The rapid increase in the frequency with which artificially modified or mutated enzymes are studied is making it less and less safe to assume that enzymes are stable under assay conditions, and there is thus an increased need for methods to check for enzyme stability, and a method for doing this is briefly described. Finally, the Scatchard plot (together with the Eadie-Hofstee plot) is used as an example to discuss the dangers of publishing derived information unaccompanied by any primary data.
Related Concept Videos
Enzyme Inhibition
Enzyme Kinetics
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Improving Translational Accuracy
Introduction to Enzyme Kinetics
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
Catalytically Perfect Enzymes
Introduction to Mechanisms of Enzyme Catalysis

