The α2 chain of rat skin collagen was cleaved at methionyl bonds with cyanogen bromide. The digest was fractionated by ion-exchange and molecular sieve chromatography and six peptides were isolated in approximately equimolar amounts. Each peptide represents a unique portion of the α2 chain as shown by chromatographic properties, amino acid analysis, and molecular weight. Together they account for all the amino acids of the α2 chain and its molecular weight of about 95,000. The peptides include a tripeptide, a tetradecapeptide, a peptide of 30 residues, and three large peptides each of about mol wt 30,000. © 1969, American Chemical Society. All rights reserved.