| Literature DB >> 3518704 |
R W Mason, D A Johnson, A J Barrett, H A Chapman.
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.Entities:
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Year: 1986 PMID: 3518704 PMCID: PMC1153120 DOI: 10.1042/bj2330925
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857