Isolation, characterization and comparative studies of the N-terminal peptides from soluble pig skin collagen.

Collagen is an ubiquitous structural protein, which constitutes about 25-30% by weight of all proteins in the mammalian body. It functions as an important supporting element in vertebrate tissues. Using the method of cleaving the protein chains at the methionyl residues with cyanogen bromide (CNBr), many species of collagen from different sources have been isolated and characterized, e.g. rat skin [l ,2] , chick skin [3] , calf skin [4,5] and human skin collagen [6] . Pig skin collagen seems to be interesting from the point of view, that is, its applicability in the medical sector [7,11,12] , due to its poor or non-antigenic reactivity. We reported previously about the isolation and characterization of the large CB-peptides derived from both oiland cw2-chain of the pig skin collagen [8]. This report deals with the isolation, characterization and comparison of the N-terminal CB-peptides of soluble pig skin collagen with the corresponding peptides derived from rat skin, calf skin and human skin collagen.