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Studies of collagen from experimental animals have led to a considerable understanding of the biological function and mode of biosynthesis of this important connective tissue protein (2, 3). The amino acid composition and sequence of collagen (3, 4), the helical structure of the triplestranded collagen monomer (4, 5), and the relationship between collagen and gelatin (4) have also been subjects of intensive investigation. Soluble collagen, when denatured by heat to break secondary bonds, has been shown to exist mainly in the form of a (single-chain) and /8 (doublechain) components (6-8). There is evidence indicating that two of the chains (al) comprising the collagen monomer are identical in amino acid composition whereas the third (a2) is different (9-11) .1 Although a number of linkages have been proposed (4), the nature of the covalent bonds involved in the intramolecular cross-linking of collagen and the relationship, if any, of such bonds to intermolecular cross-links have not been conclusively established. Although distinct species differences in collagen chemistry have been demonstrated, it is reasonable to expect that much of the information obtained from the examination of other mammalian collagens will have direct relevance to the study of the protein in humans. However, the precise ap-

A Biochemical Study of Human Skin Collagen and the Relation between Intra- and Intermolecular Cross-Linking *