Abstract
The enzyme phenol oxidase was purified from carrot cells in an apparent inactive form, prophenol oxidase, to electrophoretic homogeneity. The proenzyme had a M r of ca 36 000 under non-reducing as well as reducing conditions as judged by SDS-PAGE. Phenol oxidase activity of the purified prophenol oxidase could be induced by the addition of calcium chloride at millimolar concentration, or by trypsin treatment.
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.
