RT Journal Article
T1 Purification and Characterization of Two Isolectins with Arginase Activity from the Lichen Xanthoria parietina
A1 Molina Millán, María del Carmen
A1 Vicente Córdoba, Carlos
AB Two 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.
PB BSRK & Springer-Verlag
SN 0219-1024
YR 2000
FD 2000-07
LK https://hdl.handle.net/20.500.14352/57929
UL https://hdl.handle.net/20.500.14352/57929
LA eng
NO Dirección General de Investigación Científica y Tecnológica
DS Docta Complutense
RD 15 may 2024