The resolution of Ascaris cuticle collagen into three chain types

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Abstract
Reduced and methylated collagen from A. lumbricoides cuticle was resolved into 3 major components by chromatography on phosphocellulose. The components have similar molecular weights of about 52,000 by sedimentation equilibrium and molecular sieve chromatography, but they have different amino acid compositions. Since they do not appear to be stoichiometrically related, they apparently represent chains from collagens of more than 1 type. All 3 chains contain about 27 residue % glycine, 36 residues of proline, and 17 residues of methylcysteine, suggesting that the collagens can be maximally about 80% triple helical and are extensively disulfide cross-linked in the native state. Two minor components from the cuticle are apparently derived from 1 of the major chains by cleavage in a single region to give 2/3 and 1/3 fragments.