Arachis hypogaea lectin

Lectin PNA Arachis hypogaea Lectin RCA 120 Ricinus communis Lectin SNA Sambucus nigra... 

Arachis hypogaea lectin Bandeiraea simplicifolia lectin... 

An affinity matrix produced by cross-linking arabinogalactan with epichloro-hydrin has been used in the large scale preparation of peanut Arachis hypogaea) lectin. Many of the macromolecular properties of this lectin have been found to conform to general properties observed for numerous other plant lectins. At pH 8, the lectin exists as a compactly folded tetramer (mol. wt. 9.8 X 10 ) but at low pH it exists as a globular dimer. In dissociating solvents,... 

R. Lotan, E. Skutelsky, D. Danon, and N. Sharon, The purification, composition, and specificty of the anti-T lectin from peanut (Arachis hypogaea), J. Biol. Chem., 250 (1975) 8518-8523. 

Arachis lectin (= Peanut Arachis hypogaea (peanut) [T CCK release T... 

Arachis lectin (agglutinin) Arachis hypogaea (peanut) Gal, Glc, Man,... 

Movement of the biological material ricin with soil-size fractions are shown in Figures 4.6 and 4.7. Studies on peanut (Arachis hypogaea) seed lectin show similar results (Zartman et al. 2005). These lectin data are similar in distribution to published values (Ravi et al. 2004). The inhalation of dust generated from ricin-contami-nated soils could pose a serious hazard to war fighters. Work of A. H. Corwin cited in Lamanna (1961) stated that ricin particles with a median diameter of 2 /(ui are 2.75 times as toxic as particles with a maximal particle size of 4.2 pm. 

The peanut Arachis hypogaea) contains a lectin with anti-T (Gal(Pl-3)GalNAc) activity [174]. This antigen appears on human erythrocytes following treatment with sialidase and leads to the phenomenon known as polyagglutinability as monitored by the peanut lectin [175]. Peanut agglutinin, purified by numerous affinity purification schemes, is a tetrameric protein composed of four carbohydrate-free subunits, A/f = 27000Da[176]. The lectin is a metalloprotein rich in acidic and hydroxylic amino acids and devoid of cysteine [176]. 

The addition of specific sugars to solutions of several lectins induces u.v. difference spectra. Difference spectra for Lens culinaris, Sophora japonica, Solamm tuberosum lectins, and wheat germ agglutinin have peaks characteristic of the L-tryptophan residue, whereas that of Arachis hypogaea agglutinin has peaks characteristic of L-tyro ine residues. The binding constants for the lectins with specific sugars may be determined from the intensities of the difference spectra. Lectins may be used for the differentiation of serum enzymes. Lectins from... 

In a c.d. study of the conformation and conformational transitions of the lectins from Arachis hypogaea. Lens culinaris, Glycine max, and Ricinus communis, those of A. hypogaea and L. culinaris appear to possess a high level of pleated sheet structure in the j8-conformation. When the tertiary structure of each of the lectins became disorganized in the presence of sodium dodecyl sulphate, a new conformation was observed with a higher helical content than that found in the native protein. Dissociation into subunits may be one of the first steps in these transitions. 

Uhlenbruck, G., Pardoe, G. L, and Bird, G. W, G., 1969, On the specificity of lectins with a broad agglutination spectrum. II. Studies on the nature of the T-antigen and the specific receptors for the lectin of Arachis hypogaea, Z. Immun, Forsch. 138 423. 

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