Proteoglycan-degrading enzymes. A radiochemical assay method and the detection of a new enzyme cathepsin F

Author:

Dingle J T,Blow A M J,Barrett A J,Martin P E N

Abstract

1. Polyacrylamide beads containing entrapped 35S-labelled proteoglycan molecules have been prepared. 2. The measurement of release of radioactivity provides an extremely sensitive assay for proteoglycan-degrading enzymes, including proteinases and hyaluronidase. 3. The amount of label released is a logarithmic function of enzyme concentration or time of incubation. Experiments were made in an attempt to explain this. 4. Assays were made by the new method at several pH values, and with the inclusion of inhibitors to identify the proteoglycan-degrading enzymes of rabbit ear cartilage. 5. A previously undescribed proteinase active against proteoglycan at pH4.5 but unaffected by pepstatin, was discovered. The enzyme was named cathepsin F, and was partially purified and characterized; it was detected in human articular cartilage.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Cited by 53 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Cathepsin B as a cancer target;Expert Opinion on Therapeutic Targets;2013-01-08

2. Cathepsin F;Handbook of Proteolytic Enzymes;2013

3. Glycosaminoglycan Degradation;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

4. Selective and Signal-dependent Recruitment of Membrane Proteins to Secretory Granules Formed by Heterologously Expressed von Willebrand Factor;Molecular Biology of the Cell;2002-05

5. Human Cathepsin F;Journal of Biological Chemistry;1998-11

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