Polyreactivity as an acquired artefact, rather than a physiologic property, of antibodies: evidence that monoreactive antibodies may gain the ability to bind to multiple antigens after exposure to low pH

Michael J. McMahon, Richard O'Kennedy

    Research output: Contribution to journalArticle

    65 Citations (Scopus)

    Abstract

    Evidence is presented that monoreactive antibodies exposed to low pH may acquire the ability to bind to multiple antigens. M11, a murine, monoclonal, IgM(K) anti-goat IgG (GIgG) was purified from a hybridoma supernatant by elution at low pH from an anti-mu-Sepharose 4B affinity column. By measuring the specific antiGIgG activities and the affinity constants for the interactions of M11, pre- and post-affinity-purification, with GIgG, M11 was shown to be monoreactive before purification. Quite unexpectedly, however, the affinity-purified M11 reacted extensively with size-fractionated liver proteins when tested in an immunoblot, clearly indicating that it was polyreactive. It was concluded that the exposure to low pH had altered the M11 binding-site so as to allow it to bind to many different proteins. This phenomena provides an alternative basis for interpreting the polyreactivity observed following affinity-purification.
    Original languageEnglish
    Pages (from-to)1-10
    Number of pages10
    JournalJournal of immunological methods
    Volume241
    Issue number1-2
    DOIs
    Publication statusPublished - 31 Jul 2000

    Keywords

    • Polyreactive
    • Immunoblot
    • Affinity-purification

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