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Related Experiment Videos

Localization, characterization and partial purification of TMAO-ase

T A Gill, A T Paulson

    Comparative Biochemistry and Physiology. B, Comparative Biochemistry
    |January 1, 1982
    PubMed
    Summary

    An enzyme in cod kidney reduces trimethylamine oxide (TMAO) to formaldehyde (FA) and dimethylamine (DMA). This enzyme, TMAO-ase, is located in lysosomes and exists as at least four isozymes.

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    Area of Science:

    • Biochemistry
    • Marine Biology
    • Enzymology

    Background:

    • Formaldehyde (FA) and dimethylamine (DMA) are naturally produced in fish.
    • These compounds can affect fish quality and safety.

    Purpose of the Study:

    • To identify and characterize the enzyme responsible for reducing trimethylamine oxide (TMAO) to FA and DMA in cod.
    • To understand the enzyme's localization and properties.

    Main Methods:

    • Enzyme isolation and partial purification from cod kidney tissue.
    • Characterization of enzyme activity and properties.
    • Isoelectric focusing to separate enzyme isozymes.

    Main Results:

    • An enzyme, TMAO-ase, was identified in cod kidney responsible for TMAO reduction.
    • TMAO-ase was localized to purified cod kidney lysosomes.
    • At least four distinct isozymes of TMAO-ase were separated by isoelectric focusing.

    Conclusions:

    • Cod kidney lysosomes contain the enzyme TMAO-ase that produces FA and DMA from TMAO.
    • The presence of multiple TMAO-ase isozymes suggests complex regulation or function.

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