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Related Experiment Videos

Electrophoretically monodisperse cytochrome c oxidases.

M Heinrichs1, G Buse

  • 1Institut für Physikalische Chemie, Abteilung für Biopolymere, RWTH Aachen, FRG.

Biochemical and Biophysical Research Communications
|February 29, 1988
PubMed
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This study used gel electrophoresis to show cytochrome c oxidase is monodisperse. Enzyme structure varies with detergent, affecting its molecular weight and form (monomer/dimer).

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Cytochrome c oxidase (COX) is a crucial enzyme in cellular respiration.
  • Understanding COX structure is vital for elucidating its function.
  • Detergents are often used to solubilize and study membrane proteins like COX.

Purpose of the Study:

  • To determine the oligomeric state and molecular weight of cytochrome c oxidase preparations.
  • To investigate the influence of different detergents on enzyme structure.
  • To compare the structural properties of eukaryotic and prokaryotic COX.

Main Methods:

  • Discontinuous gradient polyacrylamide gel electrophoresis (PAGE) under nondenaturing conditions.
  • Discontinuous SDS-PAGE to analyze subunit composition.

Related Experiment Videos

  • Determination of molecular weight (Mr) corrected for bound detergent.

    • Main Results:

    • Bovine COX (9 subunits) exists as a dimer in Triton X-100 and a monomer in dodecyl maltoside.
    • Corrected Mr for bovine COX: 286,000 (Triton X-100) and 152,000 (dodecyl maltoside).
    • Paracoccus denitrificans COX (2 subunits) is a monomer in both detergents with a corrected Mr of 76,000.

    Conclusions:

    • Cytochrome c oxidase preparations are monodisperse.
    • Detergent choice significantly impacts the observed oligomeric state and molecular weight of COX.
    • COX from different organisms exhibits distinct structural characteristics.