title: A method for the measurement and characterization of protease activities responsible for extracellular or intracellular degradation of collagen precursors.
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.
mesh_terms: D000818:Animals; D002642:Chick Embryo; D003094:Collagen / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D003012:Microbial Collagenase / Q000378:metabolism; D010179:Pancreas / Q000201:enzymology; D010447:Peptide Hydrolases / Q000378:metabolism*; D011347:Procollagen / Q000378:metabolism*; D011393:Procollagen-Proline Dioxygenase / Q000378:metabolism; D013552:Swine; D013917:Thrombin / Q000378:metabolism; D013977:Tibia / Q000201:enzymology; D014316:Tritium; D014357:Trypsin / Q000378:metabolism
chemical_list: D011347:Procollagen; D014316:Tritium; D003094:Collagen; D011393:Procollagen-Proline Dioxygenase; D010447:Peptide Hydrolases; D014357:Trypsin; D013917:Thrombin; D003012:Microbial Collagenase