Further identification of human plasma glycoproteins interacting with the galactose-specific lectin Jacalin

Structural Basis for the Energetics of Jacalin–Sugar Interactions: Promiscuity Versus Specificity

“…20,21 Many O-linked glycoproteins such as asialoglycophorin A, asialofetuin, IgA, plasminogen, hemopexin and carcinoma related mucins strongly bind to jacalin. [27][28][29][30][31] In contrast, jacalin does not bind to glycoproteins such as ovalbumin, transferrin and a1-acid glycoprotein, which contain only N-linked oligosaccharides. 29 However, the recently reported binding of jacalin to arcelin 1, a glycoprotein with high mannose and complex oligosaccharides, necessitated a re-examination of the possibility of jacalin binding to N-glycans.…”

Autoantibodies in Endometriosis Sera Recognize a Thomsen–Friedenreich-like Carbohydrate Antigen

“…Haemopexin is a TF-bearing serum protein that binds to jacalin [16,41]. Most members of the matrix metalloproteinase (MMP) family contain haemopexin domains, with high level of sequence homology with plasma haemopexin [42].…”

Subproteomics in Analytical Chemistry: Chromatographic Fractionation Techniques in the Characterization of Proteins and Peptides

“…[37,48,66] Pillate and coworkers have used the lectin Jacalin, a lectin with a binding specificity for the Gal-b1!3-GalNac disaccharide, to investigate interactions of Jacalin with serum proteins. Lectins have the ability to recognize carbohydrate residues within oligosaccharides, specific combinations of oligosaccharide Subproteomics in Analytical Chemistry 2205 structures, or carbohydrate residues within a specific position in antennary complexes displayed on glycoproteins.…”