The UV-photolysis of peptides containing tyrosine (Tyr) was investigated in aqueous solutions at room temperature at 220 and 265 nm. The short-lived free radicals formed during photolysis were spin-trapped by t-nitrosobutane and identified by electron spin resonance. For N-acetyl-and N-formyl-L-Tyr and for peptides containing L-Tyr as the middle residue, photolysis at 265 nm under neutral conditions produced mainly spin-adducts due to the scission between the alpha carbon and the methylene group attached to the aromatic ring, while at 220 nm decarboxylation radicals were spin-trapped. Photolysis of di- and tripeptides at 275 nm in alkaline solutions predominantly generated deamination radicals. The radicals produced in the photolysis of the oxidized A chain of insulin were tentatively characterized by comparison with the results for di- and tripeptides.