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Enzyme assay in microsomes below zero degrees.

P Debey, C Balny, P Douzou

    Proceedings of the National Academy of Sciences of the United States of America
    |September 1, 1973
    PubMed
    Summary
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    The electron-transport chain in rat-liver microsomes retains activity below 0 degrees Celsius when using ethylene glycol as an antifreeze. This allows for enzyme assays in sub-zero conditions, expanding cryobiological research possibilities.

    Area of Science:

    • Biochemistry
    • Cryobiology
    • Enzyme kinetics

    Background:

    • Membrane-bound enzyme complexes are crucial for cellular respiration.
    • Studying enzyme activity at sub-zero temperatures presents challenges due to ice formation.
    • Ethylene glycol is a common cryoprotectant but its effect on enzyme function needs detailed study.

    Purpose of the Study:

    • To investigate the functional activity of the rat-liver microsomal electron-transport chain at sub-zero temperatures.
    • To determine the feasibility of performing enzyme assays in the presence of ethylene glycol below 0 degrees Celsius.
    • To understand the impact of cryoprotectants on multienzyme complex reactions.

    Main Methods:

    • Preparation of membrane-bound multienzyme complex from rat-liver microsomes.

    Related Experiment Videos

  • Suspension of the complex in aqueous-organic solvent containing ethylene glycol.
  • Measurement of electron transfer rates at various sub-zero temperatures.
  • Performance of individual and sequential enzyme assays under cryo-conditions.

    • Main Results:

    • Electron transfer activity was observed in the electron-transport chain at temperatures below 0 degrees Celsius.
    • Ethylene glycol at high concentrations did not completely inhibit enzyme function.
    • Enzyme assays were successfully conducted across a range of sub-zero temperatures, indicating retained enzymatic function.

    Conclusions:

    • The rat-liver microsomal electron-transport chain maintains catalytic activity in the presence of ethylene glycol at sub-zero temperatures.
    • Cryo-enzymatic assays are feasible for studying membrane-bound enzyme complexes under antifreeze conditions.
    • Findings support the potential for biochemical studies in cryo-environments without compromising enzyme function.