Abstract
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.
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Selected References
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