The Chain Compositions of Several Invertebrate Collagens

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Abstract
The chain compositions of invertebrate collagens from the foot muscle of abalone, the skins of octopus and squid, and the subcuticular membranes of swimming crab and spiny lobster, were studied by CM-cellulose chromatography of the denatured collagens and by chemical analysis and disc gel electrophoresis of their chromato-graphic fractions. These invertebrate collagens were solubilized by limited digestion with pepsin [EC 3.4.23.1] and found to be assembled from three a chains. The abalone collagen showed the chain composition [α]3, while the other four collagens had the composition [(αl)2α2] commonly found in various vertebrate collagens. The squid and lobster collagens, however, contained another species of α chain (α1'), which is chromatographically separable from al chain. Both chains have a very similar amino acid compositions and glycosylated hydroxylysine contents. These invertebrate collagens contained more glycosylated hydroxylysines (largely glucosylgalactosylhydroxylysine) than most vertebrate' collagens. In the invertebrates, α2 chains were unique in possessing higher contents of hydroxylysine and glycosylated hydroxylysines as compared with αl chains.

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