Resolution of DL-tryptophan by affinity chromatography on bovine-serum albumin-agarose columns

Bovine-serum albumin, known to have antipodal specificity in the binding of tryptophan, was selected as the affinity chromatographic matrix for the attempted chromatographic resolution of DL-tryptophan. Complete resolution was accomplished when Dl-tryptophan was chromatographed on bovine-serum albuminsuccinoylaminoethyl-Sepharose.