The protein chains of mammalian alcohol dehydrogenases typically lack free α-amino groups. The blocked N-terminal regions of the class III type of the rat (ADH-2), human (χχ) and horse enzymes were isolated by digestions with proteases, and characterized by mass-spectrometry supplemented with chemical analysis of the peptides and their redigestion fragments. Results were confirmed by synthesis of the corresponding peptides, followed by chromatographic comparisons of the native and synthetic products. The N-terminal regions of the three class III alcohol dehydrogenase subunits are homologous but differ from the class I and II enzymes in both the exact start position and the amino acid sequence, which suggests that different N-terminal structures are typical for each of the three classes.
