Abstract
THE mammalian collagen molecule is thought to be composed of two α1 and one α2 peptide chains. Alpha 1 and α2 have approximately the same molecular weight but differ in their amino-acid composition1. A mixture of α1 and α2 in the ratio of 2:1 (produced by the denaturation of neutral salt-soluble rat skin collagen) re-forms, under certain conditions suitable for renaturation, as much as 50 per cent of the rod-like collagen molecules2. It is of interest to learn whether the triple helix of the collagen molecule can also be formed from three al chains. Recently, Piez and Carrillo3 have investigated the renaturation of the isolated sub-units (α1, α2, and β12) of collagen at 15°. According to our experience these conditions are not optimal for the formation of the triple helix4.
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References
Piez, K. A., Eigner, E. A., and Lewis, M. S., Biochemistry, 2, 58 (1963).
Kühn, K., and Zimmermann, B., Arch. Biochem. Biophys., 109, 534 (1965).
Piez, K. A., and Carrillo, A. L., Biochemistry, 3, 908 (1964).
Kühn, K., Engel, J., Zimmermann, B., and Grassmann, W., Arch. Biochem. Biophys., 105, 387 (1964). Beier, G., Engel, J., and Grassmann, W., Biophysiker-Tagung Wien, 14-16.9.1964, Tagungsbericht, p. 101.
Hippel, P. H. v., and Wong, K. Y., Biochemistry, 2, 1399 (1963).
Hodge, A. J., Proc. U.S. Nat. Acad. Sci., 51, 871 (1964).
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KÜHN, K., TKOCZ, C., ZIMMERMANN, B. et al. Long-spacing Segments from Renatured α1 Sub-units of Collagen. Nature 208, 685 (1965). https://doi.org/10.1038/208685a0
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DOI: https://doi.org/10.1038/208685a0
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