Abstract
High-performance liquid chromatography (HPLC) was used to purify catalytically-active enzymes present in minor quantities in plant material. The three O-methyltransferases (S-adenosyl- l-methionine:catechol O-methyltransferases, E.C. 2.1.1.6) of tobacco leaves were subjected to high-performance ion-exchange chromatography. Excellent recovery of enzyme activity (70–100%) was obtained. HPLC was tentatively used at both analytical and preparative scales. As an analytical tool HPLC offered major advantages over conventional low-pressure ion-exchange chromatography in both speed and resolving power. For preparative purposes however, pre-purification of plant extracts by conventional means was necessary before HPLC. Purification achieved by HPLC was evidenced by electrophoretical analysis of the active fractions on sodium dodecyl sulphate—polyacrylamide slab gels.
Sign-in/Register to access full text options 
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.
