Molina Millán, María del CarmenVicente Córdoba, Carlos2023-06-202023-06-202000-070219-1024https://hdl.handle.net/20.500.14352/57929Two glycoproteins were purified and biochemically characterized from the lichen X. parietina. Both behaved as enzymes with arginase activity and haemaglutinins. Secreted arginase (SA) contained galactose and glucose in the saccharide moiety and an isoelectric point of 4.54. The algal binding-protein (ABP) had N-acetyl-glucosamine and glucose as glycosidic residues and an isoelectric point of 3.53. Both proteins had the same molecular mass (58.6 kDa) and the same qualitative amino acidic composition. The results allowed us to consider these glycoproteins as isolectins, which have significant physiological roles in the relationship between photobiont and mycobiont of symbiotic association.engjournal articlerestricted access577.1577.2581.1Algal binding-proteinglycoproteinisolectinssecreted arginaseBiología molecular (Biología)Bioquímica (Biología)Fisiología vegetal (Biología)2415 Biología Molecular2302 Bioquímica2417.19 Fisiología Vegetal