The ultraviolet absorption of the proteins in the region above 2500 A. comprises a broad band with its maximum about 2800 A. The spectrophotometric studies of Judd Lewis (1), Smith (2), and Smith and Marrack (3) have indicated the main quantitative features of this band without, however, disclosing evidence of finer structure. Indeed, with the exception of Spiegel-Adolf and Krumpel (4), who were able to distinguish several maxima in the absorption band of serum albu. rain, those investigators who have used the arc between metallic electrodes, in air, as the source of radiation have not discovered any details of structure. Vl~s and Prager (5) on the other hand found a band system consisting of nine narrow bands in serum albumin, when using the hydrogen discharge tube, which emits a continuous spectrum in the ultraviolet. With such a tube as source Ross (6) has Observed a similar resolution in the absorption bands of gelatin and several other proteins, and Lavin and Northrop (7) have found narrow bands in the absorption of crystalline pepsin.The ultraviolet absorption of the amino acids has likewise been extensively investigated. Although the aliphatic amino acids do not show appreciable absorption above 2500 A., the aromatic amino acids tyrosin, tryptophan, and phenylalanine give absorption in the same spectral region as the proteins, as shown by Dh6r6 (8), Ward (9), Smith (2), Gr6h and Han~k (10) and others. The absorption band of the proteins has in consequence been generally attributed to the content of these amino acids.