Nachweis der Zunahme der Bindung von Hydroxyprolin im Collagen der Haut mit dem Alter

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Abstract
The corium of cow skin is an excellent object for the study of thermic contraction of collagen fibres. It consists of a convolute of fibers with helical structure. Microscopic observation of isolated fibers in Ringer''s solution shows at heating thermic contraction at 58 to 61[degree]C. In distilled water this temperature shifts to about 5[degree]C higher. During thermic contraction (or at 65[degree]C in 10 minutes) hydroxyproline is split of collagen. A small part of it can be tested directly in the surrounding fluid and about 10 to 20 times as much after hydrolysis. The older the animal, the less hydroxyproline of the corium is liberated at 65[degree]C. The total hydroxyproline content of the corium is not different at different ages. It is concluded that with aging increased interchain crosslinking with hydrogen bounds on hydroxyproline developed, according to Gustavson''s views. This change of collagen structure may be used as a test for biological age of the collagen of the skin (corium).