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. 1986 Feb 1;233(3):925-7.
doi: 10.1042/bj2330925.

Elastinolytic activity of human cathepsin L

R W Mason, D A Johnson, A J Barrett, H A Chapman

Elastinolytic activity of human cathepsin L

R W Mason et al. Biochem J. .

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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References

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