"Collagenase" Activity of Cathepsins.
- 1 October 1954
- journal article
- research article
- Published by Frontiers Media SA in Experimental Biology and Medicine
- Vol. 87 (1), 125-128
- https://doi.org/10.3181/00379727-87-21308
Abstract
Papain and ficin digest collagen at pH 2.0 - 4.5 at low salt concentration. Collagen undergoes a reversible alteration at low pH which renders it susceptible to digestion by a number of proteolytic enzymes active at acid pH''s. A mechanism for enzymatic breakdown of collagen in areas of suppuration is suggested. No evidence was obtained to support preliminary alteration in collagen as part of the mechanism by which Clostridium histolyticum collagenase preparations degrade collagen.Keywords
This publication has 4 references indexed in Scilit:
- A MODIFIED PHOTOMETRIC NINHYDRIN METHOD FOR THE ANALYSIS OF AMINO AND IMINO ACIDSJournal of Biological Chemistry, 1953
- The activity of Clostridium histolyticum proteinase on synthetic substratesArchives of Biochemistry and Biophysics, 1953
- The relative metabolic inertia of tendon collagen in the ratBiochemical Journal, 1951
- THE ESTIMATION OF PEPSIN, TRYPSIN, PAPAIN, AND CATHEPSIN WITH HEMOGLOBINThe Journal of general physiology, 1938