Abstract
The hydrolysis of a tritiated elastin substrate by the human cysteine proteinases cathepsins B and L has been studied. Cathepsin L was found to be at least 100-fold more active on this substrate than cathepsin B. The specific activity of cathepsin L at pH 5.5 for hydrolysis of elastin was about the same as that of pig pancreatic elastase at its optimum pH of 8.8.
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CITATION STYLE
APA
Mason, R. W., Johnson, D. A., Barrett, A. J., & Chapman, H. A. (1986). Elastinolytic activity of human cathepsin L. Biochemical Journal, 233(3), 925–927. https://doi.org/10.1042/bj2330925
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