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A novel conformation-dependent monoclonal antibody specific to the native structure of beta-lactoglobulin and its application


, : A novel conformation-dependent monoclonal antibody specific to the native structure of beta-lactoglobulin and its application. Journal of Dairy Science 89(3): 912-921

Molten globules are thought to be general intermediates in protein folding and unfolding. {szligbeta}-lactoglobulin ({szligbeta}-LG) is one of the major bovine whey proteins, constituting approximately 10 to 15% of total milk proteins. We have recently identified {szligbeta}-LG as a superior marker for evaluating thermally processed milk. Strand D of {szligbeta}-LG participates in irreversible thermal unfolding as probed by a monoclonal antibody (mAb) specific to thermally denatured {szligbeta}-LG. In the present study, we used native {szligbeta}-LG as an immunogen to test the hypothesis that a specific mAb against the native {szligbeta}-LG could be established. As result, a mAb (4H11E8) directed against the native structure of {szligbeta}-LG was made. The antibody did not recognize the heat-denatured form of {szligbeta}-LG, such as its dimer and aggregates. Immunoassay using this "native" mAb showed that the stability of {szligbeta}-LG was at temperatures

US$19.90

PMID: 16507685

DOI: 10.3168/jds.S0022-0302(06)72156-7


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