RT Journal Article
ID 0ddbfe6d576a4b33
A1 Alborés, Silvana
A1 Moros, Maria
A1 Cerdeiras, María Pía
A1 de la Fuente, Jesus Martinez
A1 Grazu, Valeria
A1 Fraguas, Laura Franco
T1 A Lectin Purified from Blood Red Bracket Mushroom, Pycnoporus sanguineus (Agaricomycetidae), Mycelium Displayed Affinity Toward Bovine Transferrin
JF International Journal of Medicinal Mushrooms
JO IJM
YR 2016
FD 2016-03-09
VO 18
IS 1
SP 67
OP 74
K1 medicinal mushrooms
K1 lectin
K1 Pycnoporus sanguineus
K1 purification
K1 nanoparticles
K1 affinity adsorbent
K1 glycoproteins
AB Fungal lectins constitute excellent ligands for development of affinity adsorbents useful in affinity chromatography. In this work, a lectin was purified from Pycnoporus sanguineus (PSL) mycelium using 3 procedures: by affinity chromatography, using magnetic galactosyl-nanoparticles or galactose coupled to Sepharose, and by ionic exchange chromatography (IEC). The highest lectin yield was achieved by IEC (55%); SDS-PAGE of PSL showed 2 bands with molecular mass of 68.7 and 55.2 kDa and IEC displayed 2 bands at pi 5.5 and 5.2. The lectin agglutinates rat erythrocytes, exhibiting broad specificity toward several monosaccharides, including galactose. The agglutination was also inhibited by the glycoproteins fetal calf fetuin, bovine lactoferrin, bovine transferrin, and horseradish peroxidase. The lectin was then used to synthesize an affinity adsorbent (PSL-Sepharose) and the interaction with glycoproteins was evaluated by analyzing their chromatographic behaviors. The strongest interaction with the PSL-derivative was observed with transferrin, although lower interactions were also displayed toward fetuin and lactoferrin. These results indicate that the purified PSL constitutes an interesting ligand for the design of affinity adsorbents to be used (i.e., in glycoprotein purification).
PB Begell House
LK https://www.dl.begellhouse.com/journals/708ae68d64b17c52,33df00905b660ea5,0ddbfe6d576a4b33.html