Swamy, MJ and Gupta, D and Mahanta, SK and Surolia, A (1991) Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin. In: Carbohydrate Research, 213 . pp. 59-67.
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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 -57.04 kJ·mol-1 and -118.1 J·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-G(M1) tetrasaccharide, with comparable affinity, 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-G(M1) 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.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier Science.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||30 Dec 2009 09:56|
|Last Modified:||19 Sep 2010 05:51|
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