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Anti-flavin antibodies.

M J Barber, D C Eichler, L P Solomonson

    The Biochemical Journal
    |February 15, 1987
    PubMed
    Summary
    This summary is machine-generated.

    Researchers developed antibodies against flavin adenine dinucleotide (FAD) to detect covalently bound flavin in proteins. These antibodies serve as sensitive probes for specific flavin linkages in enzymes like succinate dehydrogenase.

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    Area of Science:

    • Biochemistry
    • Immunology
    • Enzymology

    Background:

    • Flavin adenine dinucleotide (FAD) is a crucial coenzyme in various enzymatic reactions.
    • Detecting covalently bound FAD in proteins is essential for understanding enzyme function and regulation.

    Purpose of the Study:

    • To generate and characterize antibodies specific to flavin adenine dinucleotide (FAD).
    • To evaluate the utility of anti-FAD antibodies as probes for detecting covalently bound FAD in proteins.

    Main Methods:

    • Antibodies were elicited against N-6-(6-aminohexyl)-FAD conjugated to bovine serum albumin.
    • Antibody cross-reactivity was assessed using Ouchterlony double-diffusion analysis.
    • Partial purification of anti-FAD IgG was performed using ammonium sulfate precipitation and various chromatography techniques.

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  • Immuno-blotting was employed to detect covalently bound FAD in flavin-containing enzymes.

    • Main Results:

    • Partially purified anti-FAD IgG did not inhibit the catalytic activity of flavin-containing enzymes.
    • Anti-FAD IgG effectively detected covalently bound FAD in proteins like succinate dehydrogenase, p-cresol methylhydroxylase, and monoamine oxidase via immuno-blotting.
    • Detection limits reached femtomolar concentrations of FAD, with higher sensitivity for the 8 alpha-N(3)-histidyl linkage compared to 8 alpha-O-tyrosyl substitution.

    Conclusions:

    • Anti-FAD IgG antibodies are specific probes for detecting covalently bound FAD.
    • These antibodies enable sensitive detection of specific flavin-protein linkages, aiding in the study of flavoenzymes.