Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Introduction to Enzyme Kinetics

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
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...

Enzyme Kinetics

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
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...

Determination of Michaelis Constant and Maximum Elimination Rate

Determination of Michaelis Constant and Maximum Elimination Rate

The Michaelis constant (KM) and the theoretical maximum process rate (Vmax) are vital parameters in the Michaelis-Menten equation, central to many biochemical reactions. They provide essential insights into enzyme kinetics and drug metabolism.
These parameters can be estimated by analyzing plasma concentration data post-drug administration. A notable example of this application is phenytoin, a drug with capacity-limited kinetics. It's recommended that phenytoin should be administered at two...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Monitoring macroplastics in aquatic and terrestrial ecosystems: Expert survey reveals visual and drone-based census as most effective techniques.

The Science of the total environment·2024

Same author

Bioindicator species of plastic toxicity in tropical environments.

The Science of the total environment·2024

Same author

Assessing marine litter in a highly polluted area in the Mediterranean: A multi-perspective approach in the Saronikos Gulf, Greece.

Marine pollution bulletin·2024

Same author

Paraffin waxes in the North-Western Mediterranean Sea: A comprehensive assessment in the Pelagos Sanctuary, a Specially Protected Area of Mediterranean Importance.

Journal of hazardous materials·2024

Same author

Characterization of floating microplastic contamination in the bay of Marseille (French Mediterranean Sea) and its impact on zooplankton and mussels.

Marine pollution bulletin·2022

Same author

Lessons learned from an intercalibration exercise on the quantification and characterisation of microplastic particles in sediment and water samples.

Marine pollution bulletin·2020

Search research articles

Related Experiment Video

Updated: Jul 3, 2026

Kinetic Screening of Nuclease Activity using Nucleic Acid Probes

Kinetic Screening of Nuclease Activity using Nucleic Acid Probes

Published on: November 1, 2019

Routine determination of enzyme kinetics using plate reader.

F Galgani¹, Y Cadiou, G Bocquene

¹IFREMER/DERO.MR-Department Milieu et Resources, BP 1049 F. 44037 Nantes Cedex 01, France.

Biotechnology and Bioengineering

|August 5, 1991

Summary

This study presents a Turbo Pascal program for routine determination of enzyme kinetics parameters (K(m) and V(max)) using a 96-well microtiter plate reader, simplifying data analysis and visualization.

More Related Videos

Determination of Microbial Extracellular Enzyme Activity in Waters, Soils, and Sediments using High Throughput Microplate Assays

Determination of Microbial Extracellular Enzyme Activity in Waters, Soils, and Sediments using High Throughput Microplate Assays

Published on: October 1, 2013

A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors

A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors

Published on: August 17, 2019

Related Experiment Videos

Last Updated: Jul 3, 2026

Kinetic Screening of Nuclease Activity using Nucleic Acid Probes

Kinetic Screening of Nuclease Activity using Nucleic Acid Probes

Published on: November 1, 2019

Determination of Microbial Extracellular Enzyme Activity in Waters, Soils, and Sediments using High Throughput Microplate Assays

Determination of Microbial Extracellular Enzyme Activity in Waters, Soils, and Sediments using High Throughput Microplate Assays

Published on: October 1, 2013

A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors

A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors

Published on: August 17, 2019

Area of Science:

Biochemistry
Enzymology
Analytical Chemistry

Background:

Enzyme kinetics are crucial for understanding enzyme function and drug development.
Traditional methods for determining enzyme kinetics parameters can be time-consuming and complex.
Microtiter plate readers are widely available and suitable for high-throughput assays.

Purpose of the Study:

To develop a user-friendly method for routine determination of enzyme kinetics parameters.
To implement a software solution for analyzing colorimetric enzyme reaction data.
To validate the accuracy of the determined kinetic parameters.

Main Methods:

Utilized a 96-well microtiter plate reader for colorimetric enzyme reactions.
Developed a Turbo Pascal program for data analysis, including plate format description, assay condition definition, and data collection.
Employed iterative determination, Lineweaver-Burk, and Hofster transformations for K(m) and V(max) calculation.

Main Results:

The developed system successfully measures and analyzes enzyme kinetics parameters.
Calculated kinetic parameters (K(m) and V(max)) with associated standard errors.
Demonstrated the system's capability for routine determination of kinetic parameters.

Conclusions:

The described method and software provide an efficient approach for routine enzyme kinetics analysis.
This system is applicable to various colorimetric enzyme assays.
The approach simplifies data processing and enhances the accessibility of kinetic parameter determination.