DOI: 10.1042/bj2330925. Elastinolytic activity of human cathepsin L

Elastinolytic activity of human cathepsin L

10.1042/bj2330925

Crossref journal-article

Portland Press Ltd.

Biochemical Journal (288)

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.

Bibliography

Mason, R. W., Johnson, D. A., Barrett, A. J., & Chapman, H. A. (1986). Elastinolytic activity of human cathepsin L. Biochemical Journal, 233(3), 925â927.

Authors 4

R W Mason (first)
D A Johnson (additional)
A J Barrett (additional)
H A Chapman (additional)

References 0 Referenced 140

None

Dates

Type	When
Created	10 years ago (Aug. 10, 2015, 4:52 p.m.)
Deposited	3 years, 9 months ago (Nov. 25, 2021, 11:30 a.m.)
Indexed	1 day, 17 hours ago (Sept. 3, 2025, 6:42 a.m.)
Issued	39 years, 7 months ago (Feb. 1, 1986)
Published	39 years, 7 months ago (Feb. 1, 1986)
Published Print	39 years, 7 months ago (Feb. 1, 1986)

Funders 0

None

BibTeX

@article{Mason_1986, title={Elastinolytic activity of human cathepsin L}, volume={233}, ISSN={1470-8728}, url={http://dx.doi.org/10.1042/bj2330925}, DOI={10.1042/bj2330925}, number={3}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Mason, R W and Johnson, D A and Barrett, A J and Chapman, H A}, year={1986}, month=feb, pages={925–927} }

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