Abstract
Alloxazine-adenine-dinucleo-tide was prepared by the method of Warburg & Christian. The production from the substance of co-phosphorylase, after hydrolysis with N/20 HC1 and NaOH, showed that adenine was present in the molecule in the form of muscle adenylic acid. After hydrolysis with N/20 HC1 the substance retained, to a considerable extent, its ability, in combination with the protein component of the "old" yellow enzyme, to transfer hydrogen from dihydropyridine nucleotide: under the same conditions its activity as the prosthetic group of rf-amino acid oxidase was completely destroyed. This indicated the production on hydrolysis of lactoflavine-5-monophosphoric acid. Hydrolysis of the dinucleotide with acid thus results, partially, in the formation of 2 mononucleotides.

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