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

Effector binding sites in plasma amine oxidase

J B Massey, J E Churchich

    Biochimica Et Biophysica Acta
    |January 11, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Chlorpromazine binding to plasma amine oxidase alters enzyme conformation and catalytic activity. Spectroscopic and kinetic studies reveal heterogeneous binding sites and significant changes in enzyme kinetics, indicating allosteric regulation.

    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

    Mechanism of association of human plasma apolipoproteins with dimyristoylphosphatidylcholine: effect of lipid clusters on reaction rates.

    Biophysical journal·2009
    Same author

    Embryonic platelet-activating factor: an indicator of embryo viability.

    Human reproduction (Oxford, England)·2002
    Same author

    Unnatural deeds do breed unnatural troubles (Macbeth: act v, scene 1).

    Fertility and sterility·2001
    Same author

    Interaction of ceramides with phosphatidylcholine, sphingomyelin and sphingomyelin/cholesterol bilayers.

    Biochimica et biophysica acta·2001
    Same author

    Interfacial properties of phosphatidylcholine bilayers containing vitamin E derivatives.

    Chemistry and physics of lipids·2001
    Same author

    A catalytic site of protein disulfide isomerase probed with adenosine-5'-triphosphate analogs.

    Biochimica et biophysica acta·2000
    Same journal

    Cumulative Contents.

    Biochimica et biophysica acta·2020
    Same journal

    Molecular Basis of Disease Cumulative Contents.

    Biochimica et biophysica acta·2020
    Same journal

    General Subjects Cumulative Contents.

    Biochimica et biophysica acta·2020
    Same journal

    Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

    Biochimica et biophysica acta·2019
    Same journal

    Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

    Biochimica et biophysica acta·2019
    Same journal

    Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

    Biochimica et biophysica acta·2019
    See all related articles

    Area of Science:

    • Biochemistry
    • Enzyme kinetics
    • Pharmacology

    Background:

    • Plasma amine oxidase (EC 1.4.3.6) is an enzyme involved in various biological processes.
    • Chlorpromazine is a psychotropic drug with known interactions with biological systems.

    Purpose of the Study:

    • To investigate the interaction between plasma amine oxidase and chlorpromazine.
    • To elucidate the binding characteristics and kinetic effects of chlorpromazine on the enzyme.

    Main Methods:

    • Spectroscopic methods, including fluorescence spectroscopy.
    • Enzyme titration and kinetic analysis.

    Main Results:

    • Chlorpromazine binding increased the ligand's emission anisotropy.
    • Heterogeneous binding sites with dissociation constants K1 = 7.4 μM and K2 = 35 μM were identified.

    Related Experiment Videos

  • Chlorpromazine significantly altered enzyme kinetics, increasing V (5.7-fold) and modifying Km.

    • Conclusions:

    • Chlorpromazine binding induces conformational changes in plasma amine oxidase.
    • These conformational changes are transmitted to the catalytic site, affecting enzyme activity.
    • The findings suggest allosteric regulation of plasma amine oxidase by chlorpromazine.