Resolution of DL-Tryptophan by Affinity Chromatography on Bovine-Serum Albumin-Agarose Columns
- 1 October 1973
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 70 (10) , 2850-2852
- https://doi.org/10.1073/pnas.70.10.2850
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.Keywords
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