Abstract

AbstractA carboxypeptidase was partially purified from Aloe arborescens Miller var. natalensis Berger on a scale suitable for pharmacological studies. The enzyme was most active and stable at pH 5.0. The enzyme had a broad specificity against various synthetic peptides, being capable of splitting C‐terminal proline. Its activity was inhibited almost completely by diisopropylfluorophosphate, strongly by transition metals, such as Fe3+, Hg2+ and Cu2+, and moderately by sulphydryl reagents. These results indicate that Aloe enzyme is a serine carboxypeptidase and appears to contain a sulphydryl group that may be involved in its inactivation.

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 call

Disclaimer: 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.