Abstract
THERE is evidence that metal ions are involved, directly and indirectly, in the structure and function of the collagens1–11. The direct interactions between collagen proteins and metal ions must be elucidated in order to understand the roles of these ions in connective tissues. One approach is to study the metal binding properties of relatively intact collagen matrices in model systems consisting of water solutions of several ionic salts. Previous experiments have involved the binding of a few ions to purified reconstituted calf-skin collagen12, egg shell matrix13, gelatine14 and bivalent amino-acids15.
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SPADARO, J., BECKER, R. & BACHMAN, C. Size-specific Metal Complexing Sites in Native Collagen. Nature 225, 1134–1136 (1970). https://doi.org/10.1038/2251134a0
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DOI: https://doi.org/10.1038/2251134a0
Further reading
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Analyse Instrumentale Par Activation D'Albumines et D'Acides Nucleiques
Journal of Radioanalytical Chemistry (1974)
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The distribution of trace metal ions in bone and tendon
Calcified Tissue Research (1970)
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