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Related Experiment Videos

Confirmation that catalase is a glycoprotein.

M Pegg, D Crane, C Masters

    Biochemistry International
    |June 1, 1986
    PubMed
    Summary
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    Mammalian catalases from mouse, rat, and guinea pig livers contain sialic acid. This finding confirms that these catalases are glycoproteins with N-acetyl neuraminic acid in their carbohydrate structures.

    Area of Science:

    • Biochemistry
    • Glycobiology
    • Enzymology

    Background:

    • Catalases are crucial antioxidant enzymes found in many organisms.
    • The composition of mammalian catalases, particularly their carbohydrate content, is of significant interest.
    • Investigating the presence of specific sugar residues can elucidate protein function and structure.

    Purpose of the Study:

    • To determine if mammalian catalases contain sialic acid.
    • To characterize the carbohydrate moiety of purified catalases from different mammalian species.
    • To confirm the glycoprotein nature of mammalian catalases.

    Main Methods:

    • Purification of catalases from mouse, rat, and guinea pig livers.
    • Mild periodate oxidation followed by sodium boro[3H]hydride reduction.

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  • Analysis of the resulting radioactively labeled moiety using acid hydrolysis, neuraminidase treatment, ion exchange, and paper chromatography.

    • Main Results:

    • A radioactively labeled compound was generated from the treated catalases.
    • This labeled compound behaved identically to N-acetyl neuraminic acid derivatives during various analytical procedures.
    • The results indicated the presence of sialic acid in the carbohydrate portion of the enzymes.

    Conclusions:

    • Mammalian catalases are confirmed to be glycoproteins.
    • These enzymes contain variable amounts of N-acetyl neuraminic acid within their carbohydrate structures.
    • The presence of sialic acid suggests potential roles in enzyme stability, targeting, or function.