Correlationships between enzymatic activity of lectins, putrescine content and chloroplast damage in Xanthoria parietina phycobionts.

Lectins from the lichen Xanthoria parietina develop arginase activity. One of these lectins behaves as a secreted arginase whereas another is an endocellular enzyme. Both enzymes are glycosylated proteins differing in the occurrence of galactose instead of N-acetyl-D-glucosamine in secreted arginase. The affinity for the algal ligand (glycosylated cell wall urease) of secreted arginase is higher than that shown for the endocellular enzyme. When the lectin ligand is absent from the algal cell wall, both endocellular and secreted arginases seem to be able to enter algal cells. This uptake promotes the increase in the amount of algal putrescine, preferently as free polyamine, and the chloroplast is rapidly damaged. Induction of cell wall urease retains lectins outside the cells, on the cell wall, and chloroplast remains healthy.