Newly synthesized mammalian proteins contain exclusively L-amino acids. Racemization to D- amino acids occurs very slowly, the rate depending principally on the temperature and the particular amino acid. The racemization of L-aspartate to D- aspartate has been used to date long lived proteins including tooth dentine and lens crystallins [g-12]. Aspartic acid is the most useful amino acid for these purposes, the first order rate constant for racemization of metabolically stable proteins at body temperature ranging from 0.794 x 10e3/year (tooth dentine) to 1.50 x 10e3/year (myelinated white matter) [lo- 121. The percentage of D- aspartate in such metabolically stable proteins increases by about 1% for each decade. Other studies have indicated that the accumulation of D- aspartate may derive selectively from aspartate residues where the side chain carboxyl is ionized, from deamidated asparagine residues or particular amino acid sequences [8,13]. Since purified elastin is characterised by its amino acid composition, which shows only 5-9 aspartate residues/lOOO, to determine their rate of racemization presented a challenge [14]. The challenge was made more pro- found when inspection of the elastin gene sequence indicated the presence of only 3 aspartate residues amongst nearly 800 and no asparagine