ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1988.tb10214.x
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