ENZYMATIC FORMATION OF ADENYL TRYPTOPHAN: ISOLATION AND IDENTIFICATION

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Abstract
Substrate amounts of tryptophan activating enzyme were prepared from beef pancreas. Stoichiometric amounts of the enzyme, C14-L-tryptophan, and [alpha]-ATP32 were reacted, and adenyl tryptophan was isolated after denaturation of the enzyme. The properties of this compound were to be identical with those of chemically synthesized adenyl tryptophan as judged by paper chromatography, column chromatography on Dowex-1, and decomposition by hydroxylamine and water. The C14 to P32 ratio in the compound served to confirm the composition, and the enzymatic conversion to ATP demonstrated the high energy linkage. A chemical synthesis of adenyl tryptophan and an improved method for the purification of the tryptophan activating enzyme are presented.