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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