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Secreted arginases from Evernia prunastri and Xanthoria parietina thalli, exhibiting lectin activity, have been purified to homogeneity. Analyses of both amino acid and glycoside composition are reported. Purified proteins have been subjected to tryptic digestion and some amino acid sequences have been analyzed. An undecapeptide from Evernia argi- nase, which shows some degree of homology with the domain to which Mn 2+ binds, a heptapeptide and an undecapeptide from Xanthoria arginase have been analyzed, and homologies with some arginases from other fungi and plants have been found.

A first attempt to elucidate the amino acid sequence of some lichen lectins