Abstract
Hevein, a lectin-like protein is the major protein of vacuolar structures called lutoids in the latex of rubber trees. We have shown both by in planta and ex planta studies that hevein is involved in the coagulation of latex by bringing together rubber particles. This polyvalent bridging between hevein and rubber particles is mediated by N-acetyl-D-glucosamine and involves a receptor glycoprotein of 22 kDa, which is localized on the surface of the rubber particles. The proposed role of hevein helps us to understand the mechanism of coagulation of latex and assigns a physiological intracellular function to one of the smallest lectins.
Highlights
Materials ceptor glycoproteinof 22 kDa, whichis localized on the surface of the rubber particles
Latex is the cyto- and hevein was purified from lutoids serum by high pressure liquid plasm of specialized cells, the laticifers [1].During tapping, laticifers are severed, and the latex flows out of the tree, which upon coagulation and subsequent processing leads to natural rubber
Purified hevein, was added to the diluted latex, and the extentof coagulation was measured by the change in absorbance at 600 nm as a function of time
Summary
Lent bridging between hevein and rubber particles is mediated by N-acetyl-D-glucosamine and involves a re-. Latex is the cyto- and hevein was purified from lutoids serum by high pressure liquid plasm of specialized cells, the laticifers [1].During tapping, laticifers are severed, and the latex flows out of the tree, which upon coagulation and subsequent processing leads to natural rubber. Intracellular Location and Purification of the Receptor Protein-The latex was ultracentrifuged (100,000 x g for 30 min at 4 "C) and fractionated into bottom fraction (vacuolar structures, so-called lutoids), middle solubleC-serum(mainlycytosol),and the top rubber particles as. The coagulation index was defined as thetime required to get 50% of the coagulation in invitro conditions a s described above, in the absence of any additive
Sign-in/Register to view highlights & summary 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.
