Abstract
1 Tail tendon and acid soluble skin collagen from rats kept on a copper-deficient diet has been investigated. 2 Copper deficiency markedly inhibits α1—α2 cross-link formation; the amount of the acidic fragment from the cyanogen bromide cleavage of the α1 fraction, which is assumed to contain the aldehydic component of the cross-link, is evidently decreased in preparations from copperdeficient rats. 3 The α2—α2 cross-link is probably formed by another mechanism than the α1—α2 cross-link. 4 Treatment with sodium gold thiosulphate largely restores the normal degree of cross-linking in the collagen of copper-deficient rats; the gold introduces cross-links independent of monoamine oxidase and located in the telopeptide region. 5 Iron deficiency inhibits proline hydroxylation by about 40%.
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