Peanut agglutinin

Similarly, a turbidity assay can be used to monitor the formation of cross-linked complexes in real time. Recently, Xiao-Liu Li et al. used Lac-functionalized perylene bisimide (PBI-Lac) to form a right-handed supramolecular stacking induced by the chiral Lac moieties. In the turbidity assay, the PNA lectin was applied to investigate the formation of three-dimensional chiral aggregates [48], Upon addition of PBI-Lac 

FIGURE 16.7 Structure of the fSCD-scaffolded heteroglycocluster used to study the hetero cluster effect. 

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The following is a review of recent studies in our laboratory on the interaction of soybean agglutinin and of peanut agglutinin with lymphocytes from different sources. 

There are also certain classes of cells which react with peanut agglutinin, as will be shown later on. 

One approach to this problem would be to isolate the intact lectin-receptor molecules from the cell membranes and characterize them. Work in this direction has been initiated in our laboratory, and a method for the isolation of the peanut agglutinin receptor from membranes of neuraminidase-treated human erythrocytes on a column of peanut agglutinin-polyacryl-hydrazido-Sepharose has been developed (21). The amino acid composition, D-glucosamine ancHg-galac-tosamine content, and the electrophoretic mobility on polyacrylamide gel electrophoresis in sodium... 

Examination of the separated cells, which were obtained in good yield (up to 80 percent), showed that they were fully viable (>95 percent in each fraction). In all the properties tested (surface markers, response to mitogens and immunological activities), the cells agglutinated by peanut agglutinin were essentially identical with the immunologically immature cells, whereas the nonagglutinated fraction consisted of... 

Another important assumption from the lectin binding studies was that hemopoietic stem cells in the mouse may carry receptors for both peanut agglutinin and soybean agglutinin. Evidence in support of this assumption was obtained when, with the aid of peanut agglutinin and soybean agglutinin a cell fraction was isolated from mouse bone marrow and spleen, which was enriched with hemopoietic stem cells and depleted of "graft-versus-host" activity. Furthermore, such a cell fraction could be used for successful reconstruction of irradiated allogeneic mice (3SH. ... 

Burks, A.W., Cockrell, G., Connaughton, C. et al. 1994. Identification of peanut agglutinin and soybean trypsin inhibitor as minor legume allergens. Int Arch Allergy Immunol 105 143-149. 

Inhibition of Peanut Agglutinin-Blood-group Precursor Substance Precipitation by Saccharides 98... 

Slupsky, J. R., Duggan-Keen, M., Booth, L. A., Karpas, A., Rhodes, E. G. H., Cawley, J. C., Zuzel, M. (1993). The peanut-agglutinin (PNA)-binding surface components of malignant plasma cells incompletely sialylated CD44 vs sialyl 2-6Tn. Brit. J. Haematol. 83, 567-573. 

Carbohydrate chains of Cl-inhibitor were identified by a binding assay using different lectins [36]. Lectins from Sambucus nigra (SNA) and Maackia amurensis (MAA), that are specific for sialic acids, were shown to bind to Cl-inhibitor. Lectin from Datura stramonium (DSA) also reacted with the inhibitor indicating complex and hybrid sugar structures. Cl-inhibitor was enzymatically desialylated and reexamined for lectin binding. SNA and MAA did not react anymore, but in addition to DSA, peanut agglutinin, which can bind to carbohydrate chains after sialic acids are removed, bound to desialylated Cl-inhibitor. Cl-inhibitor contains about 30 sialic acid residues per molecule. SDS-... 

A listing of the X-ray crystal structure (arranged in chronological order) of plant lectins is presented in Table 2 commencing with the structure of concanavalin A at 3 A resolution [38,39]. Interestingly, it was not until 1989 that a definitive high resolution X-ray crystal structure of the concanavalin A-methyl a-D-mannopyranoside complex was elucidated [40], and the most recently reported is that of peanut agglutinin [41]. Reviews on carbohydrate-protein interactions are also worthy of note [42-45]. 

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]. 

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