Elastinolytic activity of human cathepsin L
- 1 February 1986
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 233 (3) , 925-927
- https://doi.org/10.1042/bj2330925
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.This publication has 15 references indexed in Scilit:
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