Abstract
The first method for the qualitative and quantitative evaluation of extracellular and intracellular protease activities responsible for degradation of newly synthesized collagen is described. In a double incubation method, underhydroxylated collagen chains (protocollagen) serve as substrate for protease extract and then for the indicator enzyme, 4 prolyl hydroxylase. It was possible to characterize at least four types of protocollagen sites sensible to these proteases. The microsomal fraction of chick embryo liver contained a protease active on protocollagen and whose activity was similar to that of purified human synovial collagenase.
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