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Research Papers

A Lichen Lectin Specifically Binds to the γ-1,4-Polygalactoside Moiety of Urease Located in the Cell Wall of Homologous Algae

Mara Sacristán, Ana-María Millanes, María-Estrella Legaz and Carlos Vicente

volume 1 | issue 1

january/february 2006
Pages: 23 - 27

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A lectin from the lichen Evernia prunastri developing arginase activity (EC. 3.5.3.1) binds to the homologous algae that contain polygalactosilated urease (EC. 3.5.1.5) in their cell walls acting as a lectin ligand. The enzyme bound to its ligand shows to be inactive to hydrolyze of arginine. Hydrolysis of the galactoside moiety of urease in intact algae with ?-1,4-galactosidase (EC. 3.2.1.22) releases high amount of D-galactose and impedes the binding of the lectin to the algal cell wall. However, the use of ?-,4- galactosidase (EC.3.2.1.23) releases low amounts of D-galactose from the algal cell wall and does not change the pattern of binding of the lectin to its ligand. The production of glycosilated urease is restricted to the season in which algal cells divide and this assures the recognition of new phycobiont produced after cell division by its fungal partner.

We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link: