The resolution of Ascaris cuticle collagen into three chain types.
Reduced and methylated collagen from Ascaris lumbricoides cuticle was resolved into three major components by chromatography on phosphocellulose. The components have similar molecular weights of about 52,000 by sedimentation equilbrium 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 one type. All three 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 one of the major chains by cleavage in a single region to give two-third and one-third fragments.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001200:Ascaris / Q000032:analysis*; D001665:Binding Sites; D003094:Collagen / Q000302:isolation & purification; D046911:Macromolecular Substances; D008970:Molecular Weight; D011485:Protein Binding
D000596:Amino Acids; D046911:Macromolecular Substances; D003094:Collagen