Abstract
Summary
There is an inverse relationship between monoamine oxidase activity and the proportion of salt soluble collagen in connective tissues from copper-deficient and control chicks. Copper deficiency resulted in a markedly higher concentration of salt soluble collagen in aorta (4-5-fold) and tendon (2-3-fold) than in tissues from pair-fed controls. Total collagen remained relatively constant except that copper deficiency decreased the total collagen in skin. Amine oxidase activity was significantly lower in aorta, tendon, cartilage, and skin from deficient chicks while the activities in muscle and brain were not affected. Using the degree of solubility as a criterion of maturation, it was concluded that copper is essential for catalysis of collagen crosslinking.
Get full access to this article
View all access options for this article.