Title : Epitope mapping of a monoclonal antibody specific to bovine dry milk: involvement of residues 66-76 of strand D in thermal denatured beta-lactoglobulin.

Pub. Date : 2005 Feb 4

PMID : 15536085






3 Functional Relationships(s)
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1 We also show an inverse relationship between the immunoreactivity in heated beta-LG and its binding to retinol or palmitic acid. Palmitic Acid beta-lactoglobulin Bos taurus
2 Most interestingly, pH 9-10, which neutralizes the Lys groups of beta-LG, not only reduced its immunoreactivity but also its binding to palmitic acid implicating a role of Lys-69. Palmitic Acid beta-lactoglobulin Bos taurus
3 Taken together, we concluded that strand D of beta-LG participated in the thermal denaturation between 70 and 80 degrees C and the binding to retinol and palmitic acid. Palmitic Acid beta-lactoglobulin Bos taurus