The rat collagen 2 alpha chain was isolated from a transplantable Swarm chondrosarcoma following limited pepsin proteolysis. The chromatographically purified 2 alpha chain when cleaved with cyanogen bromide yields nine peptides which have been isolated and characterized with respect to their molecular weight and their amino acid composition. Eight of these peptides can be rapidly separated by gel-permeation high-performance liquid chromatography and retrieved for further purification by ion-exchange chromatography. The nine peptides are recovered in equimolar amounts and together account for a total of 1,014 amino acid residues. The features of the isolated cyanogen bromide peptides of the 2 alpha chain clearly differentiate it from other known collagen polypeptides. The possible homologies between the 2 alpha chain and other collagen alpha chains are noted. Comparison of the cyanogen bromide peptides indicates a close relationship of the 2 alpha to the alpha 1(V) chain.
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