The al and al chains of acid-soluble steer skin collagen were cleaved with CNBr and the resulting fragments were separated by ion-exchange chromatography. The sum of the amino acids of the eight peptides isolated from al are in good agreement with the amino acid composition of the αl chain. The six peptides isolated from the CNBr digested α2 chain also accounted for the amino acid content of α2. In each case, the peptides are similar and clearly homologous to the cyanogen bromide peptides previously isolated from rat skin, human skin, chicken skin, and bone collagens. However, the short, nonhelical, NH2-terminal end of the al chain is Variable in that it may lack a NH2-terminal tetrapeptide (Glu, Leu, Ser, Tyr). The dipeptide αl-CBO, present in chicken and in rat tendon, but absent in human skin collagen, is not present in bovine skin collagen.
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