Abstract
Purified chick skin collagen constituent chains were examined for the content of the aldol condensation product of two residues of α-aminoadipic δ-semialdehyde after reduction with NaBT4 and alkali hydrolysis. The single chains, α1 and α2, contained none whereas their cross-linked dimer, β12, contained one equivalent. These findings were confirmed by the similar studies performed on the peptides derived from the cross-link region of collagen by CNBr cleavage. Data presented here strongly indicate that the aldol condensation product is the intramolecular cross-link.
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