Fluorometric Demonstration of Tryptophan in Dentin and Bone Protein

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Abstract
Typical excitation and emission fluorospectral maxima of tryptophan (275 and 345 m[mu]) and tyrosine (272 and 300 m[mu]) were obtained following complete barium hydroxide hydrolysis of dentin and bone protein in alkali-resistant glass tubes. Based on these fluorescent maxima, quantification of tryptophan in these calcified proteins by relative intensities established approximately 1 residue per molecule of collagen. Attempts to confirm this finding by chemical means failed.