Soybean agglutinin

Meyer D.L., Jadhao A.G. and Kicliter E. (1996). Soybean agglutinin binding by primary olfactory and primary accessory olfactory projections in different frogs. Brain Res 722, 222-226. 

Meyer D.L., Jadhao A.G., Kiclite R., et al. (1997). Differential labelling of primary olfactory system sub-components by soybean agglutinin binding and NADOH-D histochemistry in the frog Pipa. Brain Res 762, 275-280. 

A. Dessen, D. Gupta, S. Sabesan, C. F. Brewer, and J. C. Sacchettini, X-ray crystal structure of the soybean agglutinin crosslinked with a biantennary analog of the blood group I carbohydrate antigen, Biochemistry, 34 (1995) 4933 1-942. 

Lotan, R., Pebray, H., Cacan, M., Cacan, R., and Sharon, N. (1975) Labeling of soybean agglutinin by oxidation with sodium periodate followed by reduction with [3H] borohydride. J. Biol. Chem. 250, 1955-1957. 

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. 

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. ... 

Circular Dichroism and Saccharide-Induced Conformational Transitions of Soybean Agglutinin... 

Compound 72 (SBA) is a glycopeptide of the oligomannoside type containing nine Man residues that was obtained from soybean agglutinin.101,102 The 500-MHz, H-n.m.r. spectrum of 72 (SBA) is depicted in Fig. 54, and its n.m.r.-spectral parameters are listed in Table XXVI. 

Fig. 54.—(a) Overall, 500-MHz, H-N.m.r. Spectrum of Compound 72, Obtained from Soybean Agglutinin, (b) Expanded, Structural-reporter-group Regions of the Resolution-enhanced, 500-MHz, H-N.m.r. Spectrum of Compound 72. [The bold numbers and letters refer to the corresponding residues in the structure. The relative-intensity scale of the N-acetyl-proton region differs from that of the other parts of the spectrum, as indicated.]... 

The biophysical characteristics of soybean agglutinin were first investigated by Pallansch and Liener533 with a protein preparation known to contain minor contaminants. They determined a sedimentation coefficient of 6.4 S, a diffusion coefficient of 5.72 x 10-7 cm2 sec-1, an extinction coefficient E,1, = 15.7, a molecular weight (by sedimentation) of 105,000, and an isoelectric point at pH 6.1. Catsimpoolas and Meyer540 confirmed that the isoelectric point is pH 6.0, and reported that dissociation of the lectin in phenol-acetic acid in the presence of... 

Although, on the basis of end-group analysis (1 mole ofN-terminal alanine per 30,000 g of protein in 8 M urea) and electrophoretic studies,544 the soybean agglutinin appeared to be a tetrameric protein composed of identical subunits, Lotan and coworkers546 later reported resolution of two types of subunit in the ratio of 1 1, either by electrophoresis at alkaline pH in the presence of urea or detergents, or by chromatography on DEAE-cellulose in Tris buffer, pH 7.3, with 8 M urea. 

Several groups have investigated the chemical composition of soybean agglutinin. The early amino acid analysis of Wada and coworkers534 differs considerably from the later analyses by Lis and co-workers.538,544 They found almost twice the content of serine, leucine, and lysine, and substantially increased proline than those reported by Wada and coworkers,534 whereas the contents of methionine,... 

Chemical modification of soybean agglutinin by acetylation of its amino groups resulted in little loss of agglutinating activity, whereas the protein was quite sensitive to modification of its tyrosyl residues.547 Failure of the protein to react with 2-iodoacetamide or p-(chloro-mercuri)benzoate in 6 M urea confirmed that it was devoid of sulfhydryl groups. A metalloprotein containing151 Ca2+ and Mn2+, the soybean lectin is inactivated by Al3+, Fe3+, and Pb2+, whereas Mn2+, Ba2+, Mg2+, Ag+, Li+, and K+ are without effect.532... 

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