From reaction mixtures consisting of N-acetyldehydroaminobutyric acid methyl ester and N(alpha)-acetyl-L-lysine or N(alpha)-acetyl-L-histidine, respectively, distinct amounts of the cross-link amino acids N(epsilon)-(2-amino-2-carboxy-l-methyl-ethyl)-L-lysine (lysinomethylalanin, LMeAL) and N(tau)-(2'-amino-2'-carboxy-1'-methyl-ethyl)-L-histidine (histidinomethylalanine, HMeAL) were isolated via praparative ion-exchange chromatography and identified by H-1- and C-13-nuclear magnetic resonance. In the amino acid chromatogram, both compounds eluted clearly separated from other basic amino acids. However, neither LMeAL nor HMeAL could be detected in numerous acid hydrolysates of a range of milk products. In model studies, threonine showed a significantly lower tendency for an alkali-induced beta-elimination reaction compared to serine. The reactivity of the resulting dehydroaminobutyric acid towards nucleophiles was more than tenfold lower as compared to dehydroalanine. Thus, the formation of LMeAL as well as of HMeAL during food processing is negligible.