The Journal of General Physiology, Vol 19, 739-752,
Copyright © 1936 by The Rockefeller University Press
THE STRUCTURE OF THE ULTRAVIOLET ABSORPTION SPECTRA OF CERTAIN PROTEINS AND AMINO ACIDS
Calvin B. Coulter 1,
Florence M. Stone 1, and
Elvin A. Kabat 1
1 From the Delamar Institute of Public Health, College of Physicians and Surgeons, Columbia University, New York
1. The absorption spectra of a number of proteins in the region 2500 to 3000 A. have been found to comprise from six to nine narrow bands. In consequence of variation in the relative intensity of these bands from protein to protein, the absorption curve has a characteristic configuration for each protein.
2. These bands correspond closely in position with the narrow bands which appear in the absorption spectra of tryptophan, tyrosin, and phenylalanine. Tryptophan and tyrosin each present three bands, phenylalanine shows nine.
3. The bands in the proteins are accordingly attributed to these amino acids. In the proteins the bands are displaced from the positions which they occupy in the uncombined amino acids, in most instances, by 10 to 35 A. toward longer wavelengths.
4. The absorption spectrum of Pneumococcus Type I antibody resembles that of normal pseudoglobulin but shows characteristic differences.
Accepted on September 11, 1935
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