Evaluation of Anomericrecognition in Galactose Binding Lectins Using Crosslinked Hemicellulose: A Comparative Study Through Affinity Chromatography

Abstract

The isolation of lectins by affinity chromatography with crosslinked hemicelluloses has been a common practice because of the variety of glycosides that they present, improving the isolation of different kinds of lectins, such as the galactose ligands.Lectins affinity for carbohydrates is so specific that a simple configuration of the chiral carbon can affect affinity, and there are lectins that are more related to alfa-galactosidic than beta-galactosidic residues, setting up that way, an anomeric recognition.The anomeric configuration of galactose residuesseems to have biological importance related to the behavior of some diseases and physiological processes. This work aimed to assess the anomeric recognition of two lectins reported as β-galactose ligands (PNA and ricin) and two lectins reported as α-galactose ligands (frutalin and jacalin) in two types of hemicellulose (xyloglucan of Tamarindus indica and galactomannan of Caesalpinia pulcherrima), subsequently crosslinked and used as chromatographic matrices. As a result,chromatographic profiles and retained fractions suggested preferential anomeric recognition by lectins for the hemicelluloses crosslinked. The galactomannan matrix retained 0,5mg of PNA lectin and 2,3mg of ricin lectin; meanwhile, the xyloglucan matrix retained 3,4mg of PNA and 3,2mg of ricin; results obtained by applying 5 mg of lectin. Ricin expresses a visible flexibility in anomeric recognition, while PNA shows a restricted recognition of β-galactose residues.Frutalin and jacalin did not show recognition of the xyloglucan matrix. This work proposes using hemicellulose reticles with epichlorohydrin as affinity chromatographic matrices for anomeric studies on recognizing galactose binding lectins.

Frutalin Affinity Chromatography on Sepharose Gel as a Strategy for the Identification of Possible Tumor Markers in Myelodysplastic Syndromes

“…Frutalin (FTL) is a protein in the lectin family and is obtained from the seeds of Artocarpus incisa, which specifically binds to α-D-galactose [29]. FTL has been successfully used in immunobiology research for the recognition of cancer-associated oligosaccharides with their specificity of anomeric recognition for alpha galactosidic residues [17,18,[29][30][31][32][33].…”

Frutalin Affinity Chromatography on Sepharose Gel as a Strategy for the Identification of Possible Tumor Markers in Myelodysplastic Syndromes

“…Frutalin (FTL) is a protein in the lectin family and is obtained from the seeds of Artocarpus incisa, which specifically binds to α-D-galactose [29]. FTL has been successfully used in immunobiology research for the recognition of cancer-associated oligosaccharides with their specificity of anomeric recognition for alpha galactosidic residues [17,18,[29][30][31][32][33].…”