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.
Research Article|February 01 1986
Elastinolytic activity of human cathepsin L
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Biochem J (1986) 233 (3): 925-927.
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R W Mason, D A Johnson, A J Barrett, H A Chapman; Elastinolytic activity of human cathepsin L. Biochem J 1 February 1986; 233 (3): 925–927. doi: https://doi.org/10.1042/bj2330925
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