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

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...

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Published in:Carbohydrate research Vol. 213; p. 59
Main Authors: Swamy, M J, Gupta, D, Mahanta, S K, Surolia, A
Format: Journal Article
Language:English
Published: Netherlands 25-06-1991
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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 mM at 15 degrees and delta H and delta S values of -57.04 kJ.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 beta-D-Galp-(1---3)-D-GalNAc, beta-D-Galp-(1---3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1---3)-alpha-D-GalpNAc-(1---3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1---3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1---3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1---3)-beta-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.
AbstractList 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 degrees and delta H and delta S values of -57.04 kJ.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 beta-D-Galp-(1---3)-D-GalNAc, beta-D-Galp-(1---3)-alpha-D-GalpNAcOMe, and beta-D-Galp-(1---3)-alpha-D-GalpNAc-(1---3)-Ser, as well as the asialo-GM1 tetrasaccharide, with comparable affinity, thus showing that this lectin does not discriminate between saccharides in which the penultimate sugar of the beta-D-Galp-(1---3)-D-GalNAc unit is the alpha or beta anomer, in contrast to jacalin (Artocarpus integrifolia agglutinin), another anti T-lectin which preferentially binds to beta-D-Galp-(1---3)-alpha-D-GalNAc and does not recognize beta-D-Galp-(1---3)-beta-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.
Author Gupta, D
Swamy, M J
Mahanta, S K
Surolia, A
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/1933953$$D View this record in MEDLINE/PubMed
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Snippet 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...
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StartPage 59
SubjectTerms Arachis
Binding Sites
Carbohydrate Sequence
Kinetics
Lectins - metabolism
Molecular Sequence Data
Monosaccharides - chemistry
Monosaccharides - metabolism
Oligosaccharides - chemistry
Oligosaccharides - metabolism
Peanut Agglutinin
Plant Lectins
Title Further characterization of the saccharide specificity of peanut (Arachis hypogaea) agglutinin
URI https://www.ncbi.nlm.nih.gov/pubmed/1933953
Volume 213
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