Abstract
The hydroxyproline-rich glycoprotein of plant cell walls is secreted from the cytoplasm as a soluble monomer which slowly becomes insolubilized. A tyrosine derivative, isodityrosine, is formed in the cell wall during this insolubilization and could serve as a protein-protein crosslink. Glycoprotein insolubilization is inhibited by peroxidase inhibitors and free radical scavengers, the most effective of which is L-ascorbate. These data support a hypothesis that the hydroxyproline-rich cell wall glycoprotein forms a covalently crosslinked wall network under the control of an extracellular peroxidase/ascorbate oxidase system.
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 callMore From: Biochemical and Biophysical Research Communications
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.
