The predominant protein in the embryonic chick lens, delta-crystallin, is composed of four subunits with molecular weights near 50,000. The degree to which these 4 polypeptides are the same or dissimilar was explored in delta crystallin purified from 15-day-old embryonic chick lenses by relating the numbers of methionine-containing tryptic peptides and cyanogen bromide (CNBr) peptides derived from the native protein to the average number of methionine residues per subunit. Amino acid analyses indicated that 1 mol of native delta-crystallin contains approximately 32 methionine residues, leading to an average of 8 methionine residues per subunit. Approximately equal amounts of 8 methionine-containing tryptic peptides were resolved by two-dimensional thin layer separation on cellulose sheets and by isoelectric focusing in polyacrylamide gels. Nine CNBr peptides were resolved by a combination of electrophoresis in sodium dodecyl sulfate (SDS)-polyacrylamide gels and chromatography on SDS-hydroxylapatite columns. The additive molecular weight of the 9 CNBr peptides was very close to the delta-crystallin subunit molecular weight of 50,000. Thus, the subunits of 15-day-old embryonic chick delta-crystallin have similar sequence of encoded amino acids.