Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Nonlinear Pharmacokinetics: Michaelis-Menten Equation01:18

Nonlinear Pharmacokinetics: Michaelis-Menten Equation

1.1K
The Michaelis–Menten equation is a fundamental model for describing capacity-limited kinetics in drug metabolism. It offers insights into the rate of decline of plasma drug concentration Cp over time, with Vmax and KM as pivotal parameters.
Vmax represents the maximum achievable process rate, while KM, known as the Michaelis constant, signifies the drug concentration at which the process rate reaches half its maximum. This relationship between Vmax, KM, and Cp gives rise to three distinct...
1.1K
Chemical Equations03:10

Chemical Equations

80.8K
Chemical equations represent the identities and relative quantities of substances involved in a chemical reaction. The substances undergoing reaction are called reactants, and their formulas are placed on the left side of the equation. The substances generated by the reaction are called products, and their formulas are placed on the right side of the equation. Plus signs (+) separate individual reactant and product formulas, and an arrow (→) separates the reactant and product (left and right)...
80.8K
The Nernst Equation02:59

The Nernst Equation

46.7K
Nonstandard Reaction Conditions
The interconnection between standard cell potentials and various thermodynamic parameters such as the standard free energy change ΔG° and equilibrium constant K has been previously explored. For example, a redox reaction involving zinc(II) and tin(II) ions at 1 M concentration with Eºcell = +0.291 V and ΔG° = −56.2 kJ is spontaneous.
46.7K
Thermochemical Equations02:55

Thermochemical Equations

35.8K
For a chemical reaction (the system) carried out at constant pressure – with the only work done caused by expansion or contraction – the enthalpy of reaction (also called the heat of reaction, ΔHrxn) is equal to the heat exchanged with the surroundings (qp).
35.8K
Induced-fit Model01:13

Induced-fit Model

89.0K
Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
89.0K
Clausius-Clapeyron Equation02:35

Clausius-Clapeyron Equation

62.6K
The equilibrium between a liquid and its vapor depends on the temperature of the system; a rise in temperature causes a corresponding rise in the vapor pressure of its liquid. The Clausius-Clapeyron equation gives the quantitative relation between a substance’s vapor pressure (P) and its temperature (T); it predicts the rate at which vapor pressure increases per unit increase in temperature.
62.6K

You might also read

Related Articles

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

Sort by
Same author

Relationships between trehalose metabolism and maltose utilization in Saccharomyces cerevisiae : III. Evidence for alternative pathways of trehalose synthesis.

Current genetics·2013
Same author

Stability of immobilized D-hydantoinase from Vigna angularis and repeated cycles of highly enantioenriched production of N-carbamoyl-D-phenylglycines.

Amino acids·2004
Same author

Resolution of DL-hydantoins by D-hydantoinase from Vigna angularis: production of highly enantioenriched N-carbamoyl-D-phenylglycine at 100% conversion.

Amino acids·2000
Same author

[General surgeon and breast reconstruction after mastectomy].

Minerva chirurgica·1991
Same author

Inhibition of horse liver alcohol dehydrogenase and rabbit muscle lactate dehydrogenase by phenylhydrazine.

Biomedica biochimica acta·1991
Same author

Kinetics of the reduction of oxaloacetate catalyzed by mitochondrial malate dehydrogenase of Toxocara canis muscle.

Comparative biochemistry and physiology. B, Comparative biochemistry·1991
Same journal

Corrigendum to "Integrating experimental biology, computational methods, and artificial Intelligence in anticancer drug discovery: Bridging the translational Gap" [Comput. Biol. Med. 213 (2026) 111832].

Computers in biology and medicine·2026
Same journal

Organ dose optimization for a point-of-care forearm X-ray photon-counting CT.

Computers in biology and medicine·2026
Same journal

Physics-guided transformation of breathomic feature spaces into disease-specific representations for respiratory disease classification.

Computers in biology and medicine·2026
Same journal

An AI-driven deep learning pipeline for taxonomic classification and biodiversity assessment of deep-sea environmental DNA.

Computers in biology and medicine·2026
Same journal

Rapid personalisation of cardiovascular models using invasively measured right ventricular pressure.

Computers in biology and medicine·2026
Same journal

Biologically inspired mechanisms for enhancing robustness in EEG signal modeling: Challenges, opportunities, and perspectives.

Computers in biology and medicine·2026
See all related articles

Related Experiment Video

Updated: Jan 24, 2026

Applying an eMASS Customization Program as a Research Tool to Evaluate Consumer Benefits
08:27

Applying an eMASS Customization Program as a Research Tool to Evaluate Consumer Benefits

Published on: September 27, 2019

7.2K

Pocket computer program for fitting the Michaelis-Menten equation.

E G Oestreicher, G F Pinto

    Computers in Biology and Medicine
    |January 1, 1983
    PubMed
    Summary
    This summary is machine-generated.

    This study introduces a pocket computer program for analyzing enzyme kinetics data using the Michaelis-Menten equation. The program calculates key kinetic parameters (Km and Vm) and simulates experiments for biochemical research.

    More Related Videos

    A Mouse Model of the Cornea Pocket Assay for Angiogenesis Study
    06:13

    A Mouse Model of the Cornea Pocket Assay for Angiogenesis Study

    Published on: August 18, 2011

    16.4K
    Programmed Electrical Stimulation in Mice
    07:29

    Programmed Electrical Stimulation in Mice

    Published on: May 26, 2010

    21.2K

    Related Experiment Videos

    Last Updated: Jan 24, 2026

    Applying an eMASS Customization Program as a Research Tool to Evaluate Consumer Benefits
    08:27

    Applying an eMASS Customization Program as a Research Tool to Evaluate Consumer Benefits

    Published on: September 27, 2019

    7.2K
    A Mouse Model of the Cornea Pocket Assay for Angiogenesis Study
    06:13

    A Mouse Model of the Cornea Pocket Assay for Angiogenesis Study

    Published on: August 18, 2011

    16.4K
    Programmed Electrical Stimulation in Mice
    07:29

    Programmed Electrical Stimulation in Mice

    Published on: May 26, 2010

    21.2K

    Area of Science:

    • Biochemistry
    • Enzyme kinetics
    • Computational biology

    Background:

    • The Michaelis-Menten equation is fundamental for describing enzyme kinetics.
    • Accurate determination of kinetic parameters (Km and Vm) is crucial for understanding enzyme mechanisms.
    • Non-linear regression analysis offers a robust method for fitting kinetic data.

    Purpose of the Study:

    • To present a user-friendly program for fitting the Michaelis-Menten equation to experimental data.
    • To enable calculation of kinetic parameters (Km and Vm) and their associated errors.
    • To provide a simulation tool for enzyme kinetic experiments.

    Main Methods:

    • Development of a program for Radio Shack TRS-80 and Sharp PC 1211 pocket computers.
    • Implementation of non-linear regression analysis for Michaelis-Menten equation fitting.
    • Calculation of kinetic parameters, standard errors, and residual standard error.

    Main Results:

    • The program successfully fits experimental data to the Michaelis-Menten model.
    • Accurate determination of kinetic parameters Km and Vm is achieved.
    • Standard errors and residual standard error provide measures of parameter precision.

    Conclusions:

    • The developed program offers an accessible tool for enzyme kinetic analysis on pocket computers.
    • It facilitates the precise determination of Michaelis-Menten parameters.
    • The simulation feature aids in understanding and validating kinetic models.