1. A specific collagenase from the culture medium of rabbit synovial fibroblasts was purified by gel filtration and ion-exchange chromatography. 2. The enzyme was homogenous on polyacrylamide-gel electrophoresis and showed only traces of contaminants when tested in gels with a non-specific antiserum. 3. The rabbit fibroblast collagenase could hydrolyse collagen both in solution and in fibrillar form. Viscometry showed that at 35°C the purified enzyme could hydrolyse >50 nmol of collagen/min per mg of enzyme. 4. The purified collagenase cleaved collagen in solution at either 24°or 35°C into the characteristic 1/4 and 3/4-length fragments. However, as compared with the impure enzyme, the purified enzyme at 35°C had a much decreased capacity to further degrade the initial specific cleavage products. 5. The specific rabbit collagenase had a mol. wt. of approx. 32000 as estimated by sodium dodecyl sulphate-polyacrylamide-gel electrophoresis, and 35000 by gel filtration.
Research Article|December 01 1975
Purification and properties of a specific collagenase from rabbit synovial fibroblasts
Biochem J (1975) 151 (3): 645-653.
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Z Werb, J J Reynolds; Purification and properties of a specific collagenase from rabbit synovial fibroblasts. Biochem J 1 December 1975; 151 (3): 645–653. doi: https://doi.org/10.1042/bj1510645
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