Two fluorescent fractions were found in total acid hydrolysate of elastin. The fraction with higher chromatography mobility in isopropyl alcohol/conc. ammonia/water (9 : 1 : 2) was purified by multiple preparative paper chromatography in the same solvent system, and by gel chromatography on Sephadex G-25, ion-exchange chromatography on phosphocellulose and another gel chromatography on Sephadex G-10. The purified material was chromatographically homogeneous, had an ultraviolet absorption maximum at 315 nm and exhibited a strong 320/405 nm fluorescence. 1H- and 13C-NMR spectra were in good agreement with those published previously [6] for pyridinoline, a lysine derived fluorescent compound in collagen. The major part of the fluorescent material present in acid hydrolysate of elastin was always contaminated, even after complex purification procedures. It is concluded that elastin contains several fluorophores, one of which is a cross-linking tricarboxylic amino acid with a pyridinium ring having very probably the structure of 3-(2-amino-2-carboxyethyl)-1-(5-amino-5-carboxy-2-hydroxy-pentyl)-4-(3-amino-3- carboxypropyl)-5-hydroxypyridinium. The position of 2-amino-2-carboxyethyl and 3-amino-3-carboxypropyl residues has not been definitely established and can be interchanged.