Ultra-violet Absorption Spectra of Proteins in Deuterium Oxide

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THE absorption spectra of proteins are characterized by two absorptions in the ultra-violet region, one at 2800 and the other near 2000 Å. The former has been ascribed to the phenol1,2, indole3 and phenyl groups4 of tyrosine, tryptophan and phenylalanine. The other absorption at 2000 Å. may be attributed to peptide bonds6. Since the absorption at 2800 Å. is due to the chromophoric groups of aromatic amino-acids, this absorption is absent in proteins, such as clupein, which do not contain aromatic amino-acid, and they have only one absorption near 2000 Å.

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TAKASHIMA, S. Ultra-violet Absorption Spectra of Proteins in Deuterium Oxide. Nature 187, 597–598 (1960) doi:10.1038/187597a0

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