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Affinity antibodies purified against native ovalbumin were found more reactive (higher avidity) against heat-denatured ovalbumin than against the native molecule by three different immunochemical methods. Quantitative immunoprecipitation in soluble phase revealed that more antigen-antibody complexes were insoluble with native ovalbumin than with heat-denatured ovalbumin; 25% of antibodies were still present in supernatant at equivalence as measured by ELISA. At the same conditions with heat-denatured ovalbumin, very small amounts of antibodies were precipitated while almost no activity was found in the supernatant. Classical ELISA or competitive ELISA test allowed detection down to 100 ng/mL of native ovalbumin and 10 ng/mL of denatured ovalbumin.

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Lysozymes from either egg-white or plasma were found to be different by monoclonal antibodies (mAbs). For improving texture of "foie gras" or for economical reasons, adulterants such as fresh livers from chicken or turkey or hen egg-white have been used. Duck or goose "foie gras" were not detected by anti-duck lysozyme mAbs, while positive reactions were obtained with anti-hen-egg-white lysozyme (HEWL). Similarly, anti-HEWL mAbs detected chicken or turkey fresh liver in duck or goose "foie gras" even after heating at 80°C. In 110°C heated "foie gras" only mAbs HyHEL (hybridoma antihen-egg-white lysozyme) 5 and HyHEL 10 were effective to detect fresh hen livers.