Abstract

The absorption spectra of the proteins, egg albumin, lactalbumin, and gelatin were studied and compared with those of related amino acids and simple peptides; the effect of various solvents on these compounds was investigated. A region of selective absorption at about 280 mμ, common to proteins and to simple peptides, indicates that the seat of absorption is the peptide linkage which is the main bond in such compounds. This region coincides with that characteristic of tryptophane and tyrosine. The band consists of two components, whose separation in proteins and amino acid peptides is approximately 1200 wave numbers and in anilides about 850 wave numbers. The breaking of the peptide linkage is the cause of denaturation; the energy required is about 4.4 electron volts and varies with the solvent.

© 1941 Optical Society of America

A Spectrophotometric Study of Glutathione

Gladys A. Anslow and Elisabeth Reed Lyman
J. Opt. Soc. Am. 31(2) 114-117 (1941)

The Ultraviolet Absorption Spectra of Protein Solutions1

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J. Opt. Soc. Am. 33(4) 209-218 (1943)

Far Ultraviolet Spectrophotometric Studies of Fatty Acids by Photoelectric and Spectrographic Methods*†

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J. Opt. Soc. Am. 31(3) 271-279 (1941)

The Analysis of Toluene for Benzene by an Ultraviolet Absorption of Vapor Mixtures and the Determination of Concentration of Toluene in Air by Use of the Rayleigh-Jeans Interference Refractometer*

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J. Opt. Soc. Am. 31(12) 740-742 (1941)

A Spectrophotometric Study of Thionine*

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J. Opt. Soc. Am. 31(1) 77-84 (1941)