Recent studies have revealed the existence of at least four structurally distinct types of collagen (see reviews by Gross, 1974; Gallop & Paz, 1975). Type I tropocollagen, consisting oftwo identical al(I) chains and one a2 chain, is the predominant form in bone, dentin, tendon and adult dermis, whereas type II, composed of three al(II) chains, is found in cartilage and intervertebral disc. Type III, made of three al(III) chains, is present in dermis, blood vessels and synovium, and type IV, the basement-membrane collagen, contains three al(IV) chains. It is apparent from the distribution of these collagens that some tissues contain more than one type of collagen (Bradley et al., 1974; Epstein, 1974; Seyer et al., 1974a,b; Trelstad, 1974; Eyre & Muir, 1975b,c). This heterogeneity, together with variations in the post-translational modifications of the collagen molecule and the insolubility of the collagen fibres (Henneman, 1972), complicates the study of the primary structure of tissue collagen. With a view to facilitating the study of human genetic connective-tissue diseases with suspected primary-structure anomalies of collagen (McKusick, 1972), we have developed a technique of analysing the primary structure of collagen by using highpressure liquid-chromatographic separation of the peptides released from collagen by clostridial collagenase. We describe the specific 'fingerprints' obtained by high-pressure liquid chromatography of the peptides released from human type I, II and III collagen by clostridiopeptidase A. We also show that this technique is suitable for the analysis ofminute amounts of collagen.
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Human Collagen 'Fingerprints' Produced by Clostridiopeptidase ADigestion and High-Pressure Liquid Chromatography
