Abstract
Abstract Ascorbate oxidase [AOD, EC 1.10.3.3], a copper-containing enzyme, was purified to homogeneity from cucumber fruit (Cucumis sativus) by CM-Sephadex and hydroxyapatite column chromatography and chromatofocusing. Isoelectric point (pI) of the purified enzyme was 8.3. Two other isoforms of AOD with alkaline pI values were also found. Purified AOD (MW 150,000) was a glycoprotein composed of two identical subunits (MW 70,000). N-terminal amino acid sequence was determined as Gly-Phe-Pro-Lys-Ile-Lys-His-Tyr-Lys-Trp-Asp-Val-Glu-Tyr-Met-Phe.
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.
