Antibody against branched epitope as an affinity ligand to separate the parent protein.

A peptide that contained one of the continuous epitopes of recombinant human lymphotoxin (rhLT) (amino acid residues 139-154) has been located by epitope mapping. The branched form of this peptide was synthesized by the multiple antigen peptide procedure with an octameric branched resin and was subsequently used to elicit anti-epitope antibody in rabbits. The resulting anti-epitope was then used as an immunoaffinity ligand in affinity chromatography to purify the parent protein, rhLT, from the host cell lysate directly. It is suggested that this approach would be a general way to create novel biospecific ligands for affinity separations.