CHARACTERISTICS OF INSOLUBLE PROTEIN OF TOOTH AND BONE, I. FLUORESCENCE OF SOME ACIDIC HYDROLYTIC FRAGMENTS
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NAVAL MEDICAL RESEARCH INST BETHESDA MD BETHESDA United States
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Peptides were prepared by partial acid hydrolysis of insoluble protein of tooth and bone. Cellulose column electrophoresis was employed to separate major fluorescing peptides. Using parent gelatins, peptide mixtures, and major peptides fractions of the calcified proteins the following measurements were taken u.v. absorption and fluorescent excitation and emission spectra, extinction coefficients and total fluorescence. There is evidence that tryptophan and tyrosine contribute to the material of parent gelatin which absorbs at 280 millimicrons, and are partially responsible for the fluorescence of the preparations studied here. The total fluorescence of calcified proteins occurs as a combination of excitation of three or more fluorescing molecules, tyrosine and tryptophan to the extent of their absolute concentration and another fluorophoric groups presently unidentified.