Abstract
Collagens of diverse origin have a generally similar amino acid composition, the extreme differences recorded being for Lumbricus cuticle, in which there are 12–20 hydroxyproline residues per proline ( Watson, 1958; Maser and Rice, 1962; Josse and Harrington, in press ∗∗ ∗∗ We thank Dr. W.F. Harrington for a preprint of this paper, as well as for informative discussions. and for Ascaris cuticle, in which this ratio is reversed, with about 15 proline residues per hydroxyproline ( Watson and Silvester, 1959; Josse and Harrington). In connection with studies on the synthesis and turnover of Lumbricus cuticle collagen, to be described elsewhere, we have made observations comparing the amino acid composition of cuticle collagen with that of collagen extracted from cuticle-stripped bodies in each species of worm. For both Ascaris and Lumbricus , these measurements indicate marked differences when body and cuticle collagen are compared with respect to hydroxyproline/proline ratios. To our knowledge, such large intraspecies tissue difference in collagen composition have not been reported, although only limited date are available comparing different tissues in the same species ( Tristram and Smith, 1963).
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