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LDH-IgA immunoglobulin complexes in human serum

J Biewenga, T E Feltkamp

    Clinica Chimica Acta; International Journal of Clinical Chemistry
    |February 8, 1975
    PubMed
    Summary
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    Researchers identified lactate dehydrogenase (LDH) and immunoglobulin A (IgA) complexes in human sera, even without auto-antibodies. These LDH-IgA complexes appear unrelated to typical antigen-antibody reactions.

    Area of Science:

    • Biochemistry
    • Immunology
    • Clinical Chemistry

    Background:

    • Lactate dehydrogenase (LDH) is a key enzyme in cellular metabolism.
    • Immunoglobulin A (IgA) is a crucial antibody in the immune system.
    • Abnormalities in LDH isoenzyme patterns can indicate various health conditions.

    Purpose of the Study:

    • To investigate the presence and nature of lactate dehydrogenase (LDH) and immunoglobulin A (IgA) complexes in human sera.
    • To determine the characteristics of IgA involved in these complexes.
    • To explore the potential mechanisms of LDH-IgA complex formation.

    Main Methods:

    • Analysis of human sera using electrophoresis to examine LDH isoenzyme patterns.
    • Immunochemical techniques to detect and characterize LDH-IgA complexes.

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  • Investigation of IgA light chain types and auto-antibody presence.

    • Main Results:

    • LDH-IgA complexes were detected in sera with abnormal LDH electrophoretic patterns, including missing LDH-2 bands or shifted LDH activity.
    • The IgA involved in these complexes was identified as the kappa light chain type.
    • Auto-antibodies were not found, suggesting a non-antigen-antibody mechanism for complex formation.

    Conclusions:

    • LDH-IgA complexes can occur in human sera, particularly in cases of altered LDH isoenzyme profiles.
    • The formation of these complexes does not appear to be driven by a standard antigen-antibody reaction.
    • Further research is needed to elucidate the precise biological significance and formation pathways of LDH-IgA complexes.