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[The interaction of bifunctional monoclonal antibodies with antigens studied by a radioimmunological method].

The quadroma produced bifunctional antibodies (bAbs) with double specificity to alpha-endorphin (alpha-END) and horseradish peroxidase (HRP) were compared with the parental anti-alpha-END monoclonal antibodies (mAbs) in respect to their binding to alpha-END. bAbs were purified from quadroma culture medium by sequential HRP-sepharose and alpha-END-sepharose affinity chromatography. Using radioimmunological method the affinity of the individual anti-alpha-END combining sites of bAbs was shown to be identical to that of parental mAbs. Binding to the second antigen (HRP) didn't affect binding of bAbs to alpha-END.