The nature and location of intramolecular cross-links in collagen.

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Abstract
Isolated [alpha]1 and [alpha]2 chains and [beta]12 double chains from rat skin collagen were cleaved with CNBr [cyanogen bromide] and the digests were chromatographed on phosphocellulose. Studies on the peptldes obtained Indicate that a specific lysyl residue, located in a nonhellcal region near the N-terminus of each [alpha] chain, participates in the formation of the intramolecular interchain crosslink in collagen. The [delta] -semialdehyde of [alpha]-amino adipic acid is a probable intermediate, and the cross-link itself may result from an aldol-type condensation of 2 aldehydes on adjacent chains. The data suggest that lathyrism is due to the Inhibition of an enzymatic process by which lysine in peptide linkage is converted to the aldehyde.