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 Experiment Videos

Robust regression of enzyme kinetic data.

A Cornish-Bowden, L Endrenyi

    The Biochemical Journal
    |February 15, 1986
    PubMed
    Summary

    A new method for analyzing enzyme kinetic data, without needing to know error details, performed exceptionally well in simulations. This approach offers superior or equal results compared to standard least-squares methods for inhibition and pH-activity profiles.

    Related Concept Videos

    You might also read

    Related Articles

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

    Sort by
    Same author

    Estimating product bioequivalence for highly variable veterinary drugs.

    Journal of veterinary pharmacology and therapeutics·2012
    Same author

    Bioequivalence: tried and tested.

    Cardiovascular journal of Africa·2010
    Same author

    Systems biology may work when we learn to understand the parts in terms of the whole.

    Biochemical Society transactions·2005
    Same author

    Scaling or wider bioequivalence limits for highly variable drugs and for the special case of C(max).

    International journal of clinical pharmacology and therapeutics·2003
    Same author

    The systems biology markup language (SBML): a medium for representation and exchange of biochemical network models.

    Bioinformatics (Oxford, England)·2003
    Same author

    Information transfer in metabolic pathways. Effects of irreversible steps in computer models.

    European journal of biochemistry·2001

    Area of Science:

    • Biochemistry
    • Enzyme Kinetics
    • Computational Biology

    Background:

    • Accurate fitting of theoretical models to experimental enzyme kinetic data is crucial.
    • Traditional methods often require assumptions about data weighting and error distributions.
    • Previous work by Cornish-Bowden & Endrenyi (1981) proposed a novel fitting method.

    Purpose of the Study:

    • To rigorously evaluate the performance of a previously described method for fitting enzyme kinetic data.
    • To compare the new method against established least-squares techniques using computer simulations.
    • To assess the method's applicability across different kinetic models, including inhibition and pH-activity profiles.

    Main Methods:

    • Computer simulations were employed to test the fitting method.
    • The method was applied to equations representing linear enzyme inhibition.
    • Performance was also evaluated using data for bell-shaped pH-activity profiles.

    Main Results:

    • The tested method demonstrated robust performance across all simulated conditions.
    • Results obtained were frequently superior to those from common least-squares alternatives.
    • The method's performance was never significantly worse than existing approaches.

    Conclusions:

    • The novel fitting method is a reliable and effective tool for enzyme kinetic data analysis.
    • It offers advantages over traditional least-squares methods, particularly when error characteristics are unknown.
    • The method's principles are generalizable to various kinetic models, including two-substrate kinetics.

    Related Experiment Videos