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...

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Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 42(2004), 10 vom: 01. Dez., Seite 773-9
1. Verfasser: Fontaniella, Blanca (VerfasserIn)
Weitere Verfasser: Millanes, Ana-María, Vicente, Carlos, Legaz, María-Estrella
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
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520 |a 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 
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