Concanavalin A binds to a mannose-containing ligand in the cell wall of some lichen phycobionts
Concanavalin A, the lectin from Canavalia ensiformis, develops arginase activity depending on Mn(2+). The cation cannot be substituted by Ca(2+) which, in addition, inhibits Mn(2+)-supported activity. Fluorescein-labeled Concanavalin A is able to bind to the cell wall of algal cells recently isolate...
| Veröffentlicht in: | Plant physiology and biochemistry : PPB. - 1991. - 42(2004), 10 vom: 01. Dez., Seite 773-9 |
|---|---|
| 1. Verfasser: | |
| Weitere Verfasser: | , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2004
|
| Zugriff auf das übergeordnete Werk: | Plant physiology and biochemistry : PPB |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Ligands Plant Proteins Concanavalin A 11028-71-0 Mannose PHA4727WTP |
| Zusammenfassung: | Concanavalin A, the lectin from Canavalia ensiformis, develops arginase activity depending on Mn(2+). The cation cannot be substituted by Ca(2+) which, in addition, inhibits Mn(2+)-supported activity. Fluorescein-labeled Concanavalin A is able to bind to the cell wall of algal cells recently isolated from Evernia prunastri and Xanthoria parietina thalli. This binding involves a ligand, probably a glycoprotein containing mannose, which can be isolated by affinity chromatography. Analysis by SDS-PAGE reveals that the ligand is a dimeric protein composed by two monomers of 54 and 48 kDa. This ligand shows to be different from the receptor for natural lichen lectins, previously identified as a polygalactosylated urease |
|---|---|
| Beschreibung: | Date Completed 30.06.2005 Date Revised 30.09.2020 published: Print Citation Status MEDLINE |
| ISSN: | 1873-2690 |