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Related Experiment Videos

A simple procedure for isolating adenosine triphosphatase from mitochondria.

Z Drahota, J Houstĕk

    Biochimica Et Biophysica Acta
    |June 9, 1977
    PubMed
    Summary

    A new method efficiently isolates adenosine triphosphatase (ATP synthase) from mitochondria using sonication and gel filtration. This technique successfully purifies ATP synthase from both rat liver and beef heart tissues.

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    Area of Science:

    • Biochemistry
    • Mitochondrial research
    • Enzyme purification

    Background:

    • Mitochondrial adenosine triphosphatase (ATP synthase) is crucial for cellular energy production.
    • Efficient isolation methods are needed for studying enzyme kinetics and structure.
    • Previous methods may be complex or yield lower specific activities.

    Purpose of the Study:

    • To develop a simple and effective method for isolating adenosine triphosphatase (ATP synthase) from mitochondria.
    • To characterize the specific activity of the purified enzyme from different sources.

    Main Methods:

    • Mitochondrial particles were treated with Lubrol to release the enzyme.
    • Drastic sonication was employed to further extract the enzyme.
    • Gel filtration chromatography using Sepharose 6-B was used for purification.

    Main Results:

    • The method successfully isolated adenosine triphosphatase from both rat liver and beef heart mitochondria.
    • Purified beef heart enzyme exhibited a specific activity of 120 µmol P/min per mg protein.
    • Purified rat liver enzyme showed a specific activity of 70 µmol P/min per mg protein.

    Conclusions:

    • A straightforward and effective protocol for adenosine triphosphatase isolation from mitochondria has been established.
    • The method yields highly active enzyme preparations suitable for further biochemical analysis.
    • This technique offers a valuable tool for mitochondrial enzyme research.

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