Abstract
Two methods are described for the purification of Clostridium histolyticum collagenase. One method involves gel filtration on columns of Sephadex G-200, the other, ion-exchange chromatography on DEAE Sephadex A-50. In both cases, calcium-containing buffers were found necessary for good recoveries of enzyme. Yields of collagenase activity up to 94%, free of nonspecific proteolytic activities, were consistently obtained.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
