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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

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ISSN
1437-4315
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Volume 383, Issue 7-8 (Aug 2002)

Issues

Cathepsin B Stability, But Not Activity, Is Affected in Cysteine:Cystine Redox Buffers

C. S. Pillay / C. Dennison
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2002.132

Abstract

In order to test the hypothesis that the lysosomal cysteine protease cathepsin B may be redox regulated in vivo, cathepsin B activity and stability were measured in cysteine and/or cystinecontaining buffers. Cathepsin B activity in cysteinecontaining buffers was similar at pH 6.0 and pH 7.0, over all thiol concentrations tested. In contrast, the stability of the enzyme was greater at pH 6.0 than at pH 7.0. This suggests that the enzymes operational pH in vivo may be < pH 7.0. The activity of the enzyme was depressed in glutathionecontaining buffers. When assessed in cysteine:cystine redox buffers (pH 6.0 7.0) cathepsin B was active over a broad redox potential range, suggesting that cathepsin B activity may not be redox regulated. However, at pH 7.0, the stability of cathepsin B decreased with increasing reduction potential and ambient cystine concentration. This suggests that the stability of the enzyme at neutral pH is dependent on redox potential, and on the presence of oxidising agents.

About the article

Published Online: 2005-06-01

Published in Print: 2002-08-27


Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.132.

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