Degradation of Young and Old Collagen by Extracts of Various Organs

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Abstract
In the rat uterus an enzyme is present which at acid pH and 38[degree]C degrades not only uterine collagen but also the collagen of tail tendons to fragments no longer precipitable by sulfosalicylic acid. Uterus post partum is about fivefold more active than the uterus of non-pregnant animals. With identical conditions, this enzyme degrades tendon collagen five- to sixfold faster than muscle proteins. The enzyme is not specific for the uterus. A collagen-degrading action is also found in other organs. Kidney shows the greatest activity, even greater than uterus post partum; then follow spleen, thymus, duodenum, liver and lung. All these enzymic extracts degrade tendon collagen of 5-month-old animals two- to threefold faster than that of 20-month-old animals. This supports the suggestion that during aging stronger cross-links are established in the collagen molecules.