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Sea anemone collagen: Further evidence for the existence of only oneα-chain type

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Summary

Collagen from an inferior invertebrate, namely from the sea anemoneActinia equina L., appears to consist of three identical subunits (α-chains). New evidence for this situation is reported on the basis of preparative-scale experiments.

No fractionation of sea anemone collagen was obtained by CM-cellulose chromatography which is the method of choice for the isolation of vertebrate collagen subunits. On the other hand, theα-component (mol. wt., 95.000) could be isolated by gel chromatography. It was homogenous when investigated by polyacrylamide gel electrophoresis (in the presence of sodium dodecyl sulphate) and by ion exchange chromatography on CM-cellulose. The amino acid composition of theα-component was identical with that of unfractionated collagen.

Divergent evolution of the collagen molecule appears likely since vertebrate collagen molecules are made up of differentα-chain types.

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Authors and Affiliations

  1. Max-Planck-Institut für Biochemie, D-8033, Martinsried bei München, Federal Republic of Germany

    A. Nordwig, H. Nowack & E. Hieber-Rogall

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  1. A. Nordwig
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  2. H. Nowack
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  3. E. Hieber-Rogall
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Nordwig, A., Nowack, H. & Hieber-Rogall, E. Sea anemone collagen: Further evidence for the existence of only oneα-chain type. J Mol Evol 2, 175–180 (1973). https://doi.org/10.1007/BF01653997

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  • DOI: https://doi.org/10.1007/BF01653997

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