The nonderivatized racemic mixture, DL-tryptophan, was conveniently resolved by using excellent crystalline cellulose (Avicel) for biochemical needs. Its resolution was achieved by thin layer and column chromatographies without any chemical modifications. For the purpose of knowing its resolution mechanism, DL-histidine and DL-aromatic amino acids were also chromatographed under the same conditions, which gave satisfactory separation of their enantiomers. The experimental results suggested that amino acids capable of interacting with monomeric and/or dimeric D-glucose moieties, which seem to be in the equatorial form, are more fairly resolved than those that are less interactive with the moieties.