Immunological studies of rat skin collagen were carried out with a sensitive and quantitative radioimmunoassay. Hyperimmune rabbit antisera to rat skin collagen and isolated α2 chains were used. Iodine-labeled α chains and CNBr-produced peptides served as test antigens, and native collagen, α chains, and CNBr peptides were employed as inhibitors in the assay.

The α1 and α2 chains were immunologically distinct. Although the α1 chain was not immunogenic, antibodies to α1 were detected in antisera to the intact collagen molecule. The major antigenic determinant of the α1 chain was located in α1-CB6 which constitutes the carboxy-terminal region of the chain. The α2 chain contained two non-cross-reacting antigenic determinants, one in the amino-terminal region (α2-CB1) and the other in the carboxy-terminal region (α2-CB5) of the chain. The native collagen molecule was less effective than isolated α chains in inhibiting binding of labeled peptides to antisera, indicating that antigenic determinants were less accessible in the triple helical molecule.

These immunologic studies are consistent with preliminary comparative biochemical data which indicate that interspecies structural differences in collagen predominate at both the amino- and carboxy-terminal ends of the chains.

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