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Purification and Characterization of Two Isolectins with Arginase Activity from the Lichen Xanthoria parietina

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Molina Millán, María del Carmen and Vicente Córdoba, Carlos (2000) Purification and Characterization of Two Isolectins with Arginase Activity from the Lichen Xanthoria parietina. Journal of Biochemistry and Molecular Biology, 33 (4). pp. 300-307. ISSN 0219-1024

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Abstract

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.


Item Type:Article
Uncontrolled Keywords:Algal binding-protein, glycoprotein, isolectins, secreted arginase
Subjects:Medical sciences > Biology > Molecular biology
Medical sciences > Biology > Biochemistry
Medical sciences > Biology > Plant physiology
ID Code:60757
Deposited On:03 Jun 2020 12:04
Last Modified:03 Jun 2020 12:04

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