Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin

Swamy, Musti Joginadha ; Gupta, Dipti ; Mahanta, Sanjeev K. ; Surolia, Avadhesha (1991) Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin Carbohydrate Research, 213 . pp. 59-67. ISSN 0008-6215

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Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1016/S0008-6215(00)90598-6


2-Dansylamino-2-deoxy-D-galactose (GalNDns) has been shown to bind to peanut (Arachis hypogaea) agglutinin (PNA) in a saccharide-specific manner. This binding was accompanied by a five-fold increase in the fluorescence of GalNDns. The interaction was characterized by an association constant of 0.15 mm at 15° and ΔH and ΔS values of - 57.04kJ·mol−1 and -118.1J·mol−1·K−1, respectively. Binding of a variety of other mono-, di- and oligo-saccharides to PNA, studied by monitoring their ability to dissociate the PNA-GalNDns complex, revealed that PNA interacts with several T-antigen-related structures, such as β-D-Galp-(1→3)-D-GalNAc, β-D-Galp-(1→3)-α-D-GalpNAcOMe, and β-D-Galp-(1→3)-α-D-GalpNAc-(1→3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affiity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the β-D-Galp-(1→3)-D-GalNAc unit is the α or β anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to β-D-Galp-(1→3)-α-D-GalNAc and does not recognize β-D-Galp-(1→3)-β-D-GalNAc or the related asialo-GM1 oligosaccharide. These studies also indicated that, in the extended combining region of PNA which accommodates a disaccharide, the primary subsite (subsite A) is highly specific for D-galactose, whereas the secondary subsite (subsite B) is less specific and can accommodate various structures, such as D-galactose, 2-acetamido-2-deoxy-D-galactose, D-glucose, and 2-acetamido-2-deoxy-D-glucose.

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