Despite differences in the structures of aldoses and ascorbic acid, ASA, the non‐enzymic browning of the latter involves intermediates similar to those found in Maillard browning. The kinetics of the sulphite‐inhibited browning of ASA suggest that, under anaerobic conditions, the rate of reaction of sulphite species, S(IV), is of first order with respect to S(IV). The possibility that S(IV) could catalyse the hydrolysis of the lactone ring of ASA is considered by reference to D‐glucono‐δ‐lactone. Evidence is presented to suggest that, under aerobic conditions, autoxidation of ASA leads to the oxidation of S(IV). The composition of melanoidins from ASA—glycine mixtures is compared with that from arabinose—glycine; the former contain 2.5 times more ASA‐derived residues per glycine molecule than arabinose‐derived residues per glycine molecule in the latter. The implications of these findings to the mechanism of ASA browning are discussed.