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 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.

[1]  R. Lotan,et al.  The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea). , 1975, The Journal of biological chemistry.

[2]  S. Hakomori,et al.  Monoclonal antibodies directed to the blood group A associated structure, galactosyl-A: specificity and relation to the Thomsen-Friedenreich antigen. , 1988, Molecular immunology.

[3]  I. Goldstein,et al.  Isolation and characterization of amaranthin, a lectin present in the seeds of Amaranthus caudatus, that recognizes the T- (or cryptic T)-antigen. , 1989, The Journal of biological chemistry.

[4]  J. M. Preston,et al.  Proton nuclear magnetic resonance studies of soybean lectin-monosaccharide interactions: computer analysis of complex binding behavior. , 1986, Archives of biochemistry and biophysics.

[5]  T. Osawa,et al.  Syntheses of O-β-D-galactopyranosyl-(1→3)-O-(2-acetamido-2-deoxy-α(and -β)-d-galactopyranosyl)-N-tosyl-l-serine and their interaction with d-galactose-binding lectins , 1979 .

[6]  H. Mantsch,et al.  Binding of disaccharides by peanut agglutinin as studied by ultraviolet difference spectroscopy. , 1982, European journal of biochemistry.

[7]  A. Surolia,et al.  Binding of 4-methylumbelliferyl beta-D-galactopyranoside to Momordica charantia lectin: fluorescence-quenching studies. , 1981, European journal of biochemistry.

[8]  J. Månsson,et al.  Binding specificities of the lectins from Helix pomatia, soybean and peanut against different glycosphingolipids in liposome membranes , 1983 .

[9]  H. Mantsch,et al.  Kinetics of binding of methyl alpha- and beta-D-galactopyranoside to peanut agglutinin: a carbon-13 nuclear magnetic resonance study. , 1981, Biochemistry.

[10]  A. Surolia,et al.  Analysis of Saccharide Binding to Artocarpus integrifolia Lectin Reveals Specific Recognition of T-antigen (\beta D-Gal(1\rightarrow 3)GalNAc , 1986 .

[11]  T. Irimura,et al.  Carbohydrate-binding specificity of the so-called galactose-specific phytohemagglutinins. , 1975, Carbohydrate research.

[12]  E. Kabat,et al.  Immunochemical studies on the specificity of the peanut (Arachis hypogaea) agglutinin. , 1976, Carbohydrate research.

[13]  N. Sharon,et al.  The binding of oligosaccharides containing N-acetylglucosamine and N-acetylmuramic acid to lysozyme. The specificity of binding subsites. , 1967, The Journal of biological chemistry.

[14]  G. Bird.  Anti‐T in Peanuts , 1964, Vox sanguinis.

[15]  A. Surolia,et al.  Intrinsic fluorescence studies on saccharide binding toArtocarpus integrifolia lectin , 1986, Bioscience reports.

[16]  T. Momoi,et al.  Specific interaction of peanut agglutinin with the glycolipid asialo GM1 , 1982, FEBS letters.

[17]  J. Becquart,et al.  Ultraviolet difference spectroscopy study of peanut lectin binding to Mono- and disaccharides. , 1982, Biochimica et biophysica acta.

[18]  R. Miller.  Purification of peanut (Arachis hypogaea) agglutinin isolectins by chromatofocusing. , 1983, Analytical biochemistry.

[19]  M. J. Swamy,et al.  Analysis of dynamics and mechanism of ligand binding to Artocarpus integrifolia agglutinin. A 13C and 19F NMR study. , 1988, The Journal of biological chemistry.

[20]  M. I. Khan,et al.  Thermodynamic and kinetic studies on saccharide binding to soya-bean agglutinin. , 1986, The Biochemical journal.