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Hydroxylysine in the N-terminal telopeptides of skin collagen from chick embryo and newborn rat.

The extent of hydroxylation of the single lysine residue occurring in both the oca- and OC2-CB 1 peptides obtained by cyanogen bromide cleavage of the axl- and a2-chains of collagen appears to vary according to the nature ofthe tissue from which the collagen is derived. Thus in the collagen of skin isolated from young rat and chick as in all skin collagens so far examined no hydroxylation this residue whereas in the bone from two species half the lysine converted into lysine in the collagen of membranous and tendon from chick embryos.