Key points are not available for this paper at this time.
Abstract The α1 and α2 chains of soluble collagen from human and baboon skin were separated and cleaved with cyanogen bromide, and the resultant peptides were separated by ion exchange and molecular sieve chromatography. Eight peptides from the α1 chain and six from the α2 chain accounted for the weight and amino acid content of both collagens. Only small differences of questionable significance could be detected between the collagens of the two primate species by amino acid analysis or molecular weight of the peptides. The amino-terminal cross-link region of both the α1 and α2 chain is identical in both species. The peptides are very similar to those previously isolated from the rat and the chick, demonstrating a close homology in the helical portion of the molecule and, to a lesser extent, in the amino-terminal crosslink region.
Epstein et al. (Mon,) studied this question.