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• W2047178148 abstract "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 m m 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 -Gal p -(1→3)- d -GalNAc, β- d -Gal p -(1→3)-α- d -Gal p NAcOMe, and β- d -Gal p -(1→3)-α- d -Gal p NAc-(1→3)-Ser, as well as the asialo-G M1 tetrasaccharide, with comparable affiity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the β- d -Gal p -(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 -Gal p -(1→3)-α- d -GalNAc and does not recognize β- d -Gal p -(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." @default.
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• W2047178148 date "1991-06-01" @default.
• W2047178148 modified "2023-09-26" @default.
• W2047178148 title "Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin" @default.
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• W2047178148 doi "https://doi.org/10.1016/s0008-6215(00)90598-6" @default.
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