Abstract
The β-1,3-glucanase of cultured carrot cells is found mainly in the soluble and cell wall fractions. The intracellular enzyme showed some affinity for concanavalin A and appeared to contain a mannose-rich carbohydrate moiety, while the cell wall-associated enzyme extracted by NaCl showed only a low affinity for the lectin. Secretion of the enzyme was inhibited by the addition of monensin suggesting that the enzyme is secreted via the Golgi body to the cell wall while the addition of tunicamycin did not show any significant effect on the biosynthesis and secretion into the cell wall matrix. These observations suggest that the carbohydrate moiety of the enzyme glycoprotein plays no important role in the transport and secretion of the wall-bound β-1,3-glucanase.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
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.