Almtract--A study has been made of the ultra-violet absorption spectra of purified atopic allergens at pH 2 and pH 12. The colour change of atopen solutions from deep brown in alkali to light brown or yellow in acid is reflected in the spectra by considerably higher extinction coefficients in Rlkall. By including native proteins and synthetic protein-sugar model compounds it proved possible to locate the specific differences between the spectra of the allergens in acid and alkali at wavelengths over 325 mp, i.e. in the near ultra-violet and in the visible region. It is suggested that the chemical shifts in the system: Nt-[1-deoxygiycosulosyl-(1)]-lysine residue and its 1.2-and 2.3-enolic tantomers are responsible for the colour-change phenomenon.The incorporation of these 1-amino-l-deoxy-2-ketose derivatives, especially of the 2"3-enediol form, together with their pathways of degradation in dilute solution and at extreme pH-values, provides a plausible explanation for the inactivation of solutions of atopic allergens.1. INTRODUCTION IN A previous study ~1~ the ultra-violet absorption spectra of a number of purified atopic allergens were compared with those of crystalline proteins and of synthetic model compounds, prepared by subjecting native proteins to Maillard reactions with aldose-sugars. It was found that new chromophores are introduced into the protein molecule during this reaction, giving rise to low-intensity absorption maxima at 305 mp and at wavelengths over 325 m/~. Further observations on the optical properties of systems containing e-aminocaproic acid/aldose, n-amylamine/ aldose and primary amine/~-hydroxy-aldehydes subsequently led to the conclusion that the chromophore is located at the site of a protein-sugar linkage and encompasses the nitrogen atom of the e-amino group of lysine residues in the protein and the first two (or three) carbon atoms of the aldose reactant.~2, 3~Since similar structural sites were detected optically and chemically in atopic allergens, it was concluded that these antigens characteristically contain N-substituted 1-amino-l-deoxy-2-ketoses, N~-[1-deoxyglycosulosyl-(1)-]-lysine residues, the absorption peak at 305 mt~ being attributable to the 1.2-enol form. The significance of these sites of N-glycosidic coupling in human atopic allergy became especially evident when it could be demonstrated that the specific skin-reactivity of bovine ~-hctoglobulin in atopic individuals hypersensitive to cow's milk could be increased a hundredfold by reacting the protein with lactose.~4) It is the purpose of the present article to extend the observations on the u.v. spectra of atopic allergens by differential spectroscopy at extreme pH-values and to identify derivatives of 1-amino-l-deoxy-2-ketoses incorporated in the molecular structure.