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Dilatometric, refractometric and viscometric study of lysozyme-cation interaction

C Abad, M Trueba, A Campos

    Biophysical Chemistry
    |November 1, 1981
    PubMed
    Summary

    Hen egg-white lysozyme undergoes structural changes when interacting with copper (Cu(II)) or cobalt (Co(II)) cations. These conformational alterations depend on metal ion and protein concentrations.

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    Area of Science:

    • Biochemistry
    • Biophysical Chemistry
    • Protein Science

    Background:

    • Hen egg-white lysozyme is a well-characterized enzyme with known structural and functional properties.
    • Metal cations are known to interact with proteins, potentially altering their conformation and activity.

    Purpose of the Study:

    • To investigate the interaction between hen egg-white lysozyme and Cu(II) or Co(II) cations.
    • To determine the effect of these metal cations on lysozyme's structure and conformation.

    Main Methods:

    • Dilatometry was used to obtain Delta V isotherms in copper and cobalt solutions.
    • Equilibrium dialysis-differential refractometry and viscometry were employed to measure preferential adsorption and specific viscosity.

    Main Results:

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    • The interaction between lysozyme and Cu(II)/Co(II) cations induced structural alterations in the protein.
    • The extent of these conformational changes was found to be dependent on both the type of metal ion and the protein concentration.
    • Consistent results were obtained across dilatometry, refractometry, and viscometry measurements.

    Conclusions:

    • Metal cations Cu(II) and Co(II) interact with hen egg-white lysozyme, causing significant conformational changes.
    • The observed structural modifications highlight the sensitivity of lysozyme to its ionic environment.
    • The study provides a comprehensive understanding of lysozyme-metal cation interactions using multiple biophysical techniques.