Abstract
A characteristic pattern of selective degradation of isotopically labeled collagen in tadpole tail fin in culture was observed by measuring the amount and radioactivity of degraded collagen fragments released into the culture medium as a function of time of incubation. The changes in specific activity and total amount of hydroxyproline released with time indicated early degradation apparent at 3 hr of incubation of a small fraction of newly synthesized heavily labeled collagen followed by breakdown of the bulk of old lightly labeled fibrils. Collagenase activity rose in the culture medium with the release of collagen breakdown products and continued long afterward. Serum in the medium significantly reduced the release of collagen degradation products to the medium and greatly lowered their specific activity. Possible mechanisms of selective collagen degradation are discussed.
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