Lectins soybean

JORDINSON M, DEPREZ P H, PLAYFORD R J, HEAL S, FREEMAN T 0, ALISON M, CALAM J (1996) Soybean lectin stimulates pancreatic exocrine secretion via CCK-A receptors in rats. Am J Physiol. 270 G653-9. 

There is still some discordance about markers for ATI cells [17, 18]. Varieties of glycocalyx appear to be expressed in ATI versus ATII cells, which can be distinguished by the binding of specific lectins. Lycopersicon esculen-tum lectin, for example, appears to adhere specifically to the apical plasma membrane of ATI cells [19, 20], Other lectin markers that have been reported in AEC typing are Ricinus communis agglutinin, Erythrina cristagalli lectin, soybean lectin and Bauhinia purpurea agglutinin (all for the ATI phenotype),... 

Alvarez, J.R. and Torres-Pinedo, R. 1982. Interactions of soybean lectin, soyasaponins, and glycinin with rabbit jejunal mucosa in vitro. Pediatr. Res. 16, 728-731. 

Transverse IEF was also conducted in a pressure-driven flow for BSA and soybean lectin separation on-chip [1040], Here, Pd electrodes were used (in preference to Au) because of the non-gassing character of Pd. In addition, the protein sample was sandwiched between two buffer streams and was prevented from direct contact with the channel wall (and hence the electrode), a process akin to hydrodynamic focusing [1040],... 

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... 

Tighter binding is observed if additional mannose residues are present in an oligosaccharide.The protein also has specific binding sites for Ca + and for a transition metal ion such as Mn +. Soybean lectin binds D-N-acetylgalactosamine and o-galactose units, while wheat lectin is specific for o-N-acetylglucosamine. 

The most potent inhibitor described thus far is the type A disaccharide GalNAc(al-3)Gal. However, the addition of an a-L-fucosyl group to the Gal, as occurs in the type A trisaccharide, greatly diminished its activity [168]. A hydrophobic site on soybean agglutinin was identified by its interaction with A-dansylgalactosamine [169]. The soybean lectin possesses four carbohydrate binding sites per molecule, one for each subunit [169]. 

Lectins are another class of potential antinutrient soy proteins (Sharon Lis, 1972 Liener, 1974). The carbohydrate content and structure of soy lectins were determined (Lis Sharon, 1978) and consist of mannose and Af-acetyl-glucosamine at about 5% by weight. Soy lectin has MW 110 kD from four identical subunits. The soy lectins are partly responsible for weight loss in rodent feeding studies with raw soy protein. Soy lectins are relatively easy to heat denature compared to other legume lectins. Properly processed soy foods have little native lectin present. Soybean lectins are widely used in clinical studies because of their interaction with red blood cell surface features (Friedman Brandon, 2001). 

Fasina, Y.O. H.L. Classen J.D. Garlich B.L. Black P.R. Ferket Z. Uni A.A. Olkowski. Response of Turkey poults to soybean lectin levels typically encountered in commercial diets. 2. Effect on intestinal development and lymphoid organs. Poultry Sci. 2006, 85, 870—877. 

Mining the extensive soybean EST data using the electronic Northern approach illustrates how information can be inferred about the possible sites of expression of gene family members. Here, we illustrate this approach for a small family of soybean lectins and present new information on the expression patterns of two non-seed lectins. 

GOLDBERG, R.B., HOSCHEK, G., VODKIN, L.O., An insertion sequence blocks the expression of a soybean lectin gene. Cell, 1983,33,465-475. 

LINDSTROM, J.T., VODKIN, L.O., HARDING, R.W., GOEKEN, R.M., Expression of soybean lectin gene deletions in tobacco, Devel. Genet., 1990,11, 160-167. 

PHILIP, R DARNOWSKI, D.W., MAUGHAN, P.J., VODKIN, L.O., Processing and localization of bovine beta-casein expressed in transgenic soybean seeds under control of a soybean lectin expression cassette, Plant Sci., 2001,161, 323-335. 

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