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

Buffer, pH, and ionic strength effects on the (Na+ + K+)-ATPase.

J D Robinson, R L Davis

    Biochimica Et Biophysica Acta
    |April 30, 1987
    PubMed
    Summary
    This summary is machine-generated.

    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

    Aggregation of Markov flows I: theory.

    Philosophical transactions. Series A, Mathematical, physical, and engineering sciences·2018
    Same author

    Advanced flow MRI: emerging techniques and applications.

    Clinical radiology·2016
    Same author

    THE HOT SPRINGS AT BANFF, ALBERTA.

    Canadian Medical Association journal·2010
    Same author

    Disposition of [s]-heparin in the rat.

    British journal of pharmacology and chemotherapy·2008
    Same author

    The DRD2 TaqI-B polymorphism and its relationship to smoking abstinence and withdrawal symptoms.

    The pharmacogenomics journal·2006
    Same author

    Multidimensional scaling reveals a color dimension unique to 'color-deficient' observers.

    Current biology : CB·2005
    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

    The dog kidney (Na+ + K+)-ATPase enzyme exhibits pH-dependent phosphatase activity. Free H+ ions influence enzyme conformation, affecting K+-independent and K+-activated reactions.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Membrane Transport Proteins

    Background:

    • The (Na+ + K+)-ATPase is a crucial ion pump in kidney cells.
    • This enzyme also possesses phosphatase activity, hydrolyzing p-nitrophenyl phosphate.
    • Understanding the influence of pH on these activities is vital for comprehending enzyme function.

    Purpose of the Study:

    • To investigate the effects of pH on the K+-independent and K+-activated phosphatase activities of dog kidney (Na+ + K+)-ATPase.
    • To elucidate the role of free H+ ions and buffer composition in modulating these enzymatic reactions.

    Main Methods:

    • Enzyme kinetic assays using p-nitrophenyl phosphate as a substrate.
    • Varying pH conditions (7.5 to 5.8) and employing different buffer systems (imidazole, histidine, Good buffers like Pipes and ADA).

    Related Experiment Videos

  • Analysis of enzyme activity in response to pH changes and buffer inhibition.

    • Main Results:

    • K+-independent phosphatase activity increased as pH decreased from 7.5 to 5.8.
    • K+-activated phosphatase and (Na+ + K+)-ATPase activities decreased with declining pH.
    • Specific buffers (Pipes, ADA) containing acidic groups inhibited phosphatase activity by interfering with enzyme conformational changes.

    Conclusions:

    • Free H+ ions, rather than buffer anions, primarily influence the K+-independent phosphatase activity by altering enzyme conformation.
    • The observed pH dependencies are not due to changes in substrate or cation affinity.
    • Certain buffer compounds can selectively inhibit phosphatase activity, suggesting specific interactions with enzyme conformational states.