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Clin Biochem. 2008 Oct;41(14-15):1237-44. doi: 10.1016/j.clinbiochem.2008.07.004. Epub 2008 Jul 26.

Recombinant IgY for improvement of immunoglobulin-based analytical applications.

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1
Institute of Biochemistry and Food Sciences, Division of Biochemistry and Molecular Biology University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany.

Abstract

OBJECTIVES:

In order to provide superior tools for diagnostic approaches and to prevent assay interference and background binding, the objective of this study was the establishment and evaluation of monoclonal IgY which are phylogenetically distant from mammalian immunoglobulins but have been unavailable so far.

DESIGN AND METHODS:

Human, murine and avian monoclonal model antibodies were established and produced in mammalian cells. Their interaction with human serum components and Fc gamma receptors was compared by ELISA and fluorescence activated cell sorting (FACS).

RESULTS:

The use of monoclonal IgY in contrast to mammalian antibodies prevented interference phenomena in absorbance measurements generated by human sera containing rheumatoid factor (RF) or heterophilic antibodies. Additionally, monoclonal IgY exhibited no interaction with the human and murine high-affinity receptor FCGR1 (CD64) and human low affinity receptor FCGR3a (CD16A).

CONCLUSIONS:

The data obtained demonstrate the advantageous behaviour of monoclonal IgY as detection or capture antibodies compared to conventional mammalian immunoglobulins and provide a strategy for improvement of assay performance and accuracy.

[Indexed for MEDLINE]

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