Comparative analysis of the structure and thermal stability of sea urchin peristome and rat tail tendon collagen
Journal of Cellular Biochemistry, ISSN: 0730-2312, Vol: 84, Issue: 3, Page: 567-574
2002
- 17Citations
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Article Description
We have purified collagen from two distinct sources; the vertebrate, rat tail tendon and an invertebrate, sea urchin adult tissue, the peristome. The collagenous nature of the purification products was confirmed by amino a compositional analysis. Both preparations had high contents of glycine and proline residues and hydroxyproline was also present. The total pyrrolidine (proline + hydroxyproline) content decreased from 17.9 mole % in rat tail collagen to 12.9 mole % in peristome collagen. Distinctly different circular dichroic spectra were measured for these collagens. Analyses of spectra, measured as a function of temperature, revealed distinct thermal denaturation profiles. The melting temperature for rat tail collagen was 38.5°C, while the corresponding value for peristome collagen was significantly lower at 27°C. A similar thermal denaturation profile was obtained for rat tail collagen in digestion experiments using a 41-kDa gelatinase activity, isolated from sea urchin eggs. These results identify structural differences between a typical, vertebrate type I fibrillar collagen and an echinoderm collagen which serves as a constituent of a mutable connective tissue. These differences may relate to the functional roles played by collagen in these distinctly different tissues. © 2001 Wiley-Liss, Inc.
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