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- W2488402397 abstract "This chapter describes the activity, specificity and structural chemistry of procollagen III N-proteinase. Procollagen III N-endopeptidase removes the N-terminal propeptide from native procollagen III, but neither from procollagens I or IV nor from denatured procollagen III. Cleavage is at the Tyr-Ser-Pro + Gln-Tyr-Glu-Ala bond. The activity requires calcium, but the specificity with which the enzyme cleaves procoUagen III has not been firmly established. Metal chelators and reducing agents are potent inhibitors of the enzymatic activity, whereas serine proteinase inhibitors, lysine or serum are not. Characterization at the molecular level of the enzyme responsible for the physiological procollagen III N-endopeptidase activity has not yet been performed. The enzyme has been partially purified from the culture medium of calf tendon fibroblasts, calf aortic smooth muscle cells and human placenta by using similar procedures consisting in ammonium sulfate precipitation of the conditioned culture medium or the tissue extract Procollagen III N-endopeptidase cleaves only native procoUagen III, but not heat-denatured procollagen III nor procollagen I or IV. It is found that this specificity is an intrinsic property of the enzyme or related to the assay conditions." @default.
- W2488402397 created "2016-08-23" @default.
- W2488402397 creator A5025173484 @default.
- W2488402397 date "2004-01-01" @default.
- W2488402397 modified "2023-10-13" @default.
- W2488402397 title "Procollagen III N-proteinase" @default.
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- W2488402397 doi "https://doi.org/10.1016/b978-0-12-079611-3.50128-2" @default.
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