Photolysis of pyridinoline, a cross-linking amino acid of collagen, by ultraviolet light.
Pyridinoline, a cross-linking amino acid of collagen, was degraded by irradiation of ultraviolet light. The decomposition rate varied with pH of the solution and wavelength of irradiation light. The maximum of the degradation rate at individual pH coincides with the ultraviolet absorption maximum. Namely, it was maximally degraded by irradiation at 295 nm in acidic solution and at 325 nm in neutral and alkaline solution. At the optimum wavelength, the photolysis occurred more rapidly in neutral and alkaline solution than in acidic solution. The quantum yield in neutral solution was approximately 0.11 and independent of wavelength. One of the photolysis products was identified as hydroxylysine on an amino acid analyser, indicating that the cleavage of the pyridinium ring occurred.
D000596:Amino Acids / Q000528:radiation effects*; D003094:Collagen / Q000032:analysis; D010777:Photochemistry; D013056:Spectrophotometry, Ultraviolet; D014466:Ultraviolet Rays
D000596:Amino Acids; C015484:pyridinoline; D003094:Collagen