Most people carry natural antibodies to SBA, although they do not interfere with its agglutinating properties. See: FEBS Lett 1996 Nov 18;397(2-3):139-42 SBA is a reliable marker for human eosinophils. See: Histochemistry 1987;86(3):269-73 The lectin is virtually absent from textured soy protein. See: Freed, Dietary Lectins and Disease, in Food Allergy and Intolerance (1987) Brostoff and Challacombe, ed. New York
SBA may be responsible for half of the inhibition of growth attributed to soy products. See: Arch Latinoam Nutr 1996 Dec;44(4 Suppl 1):48S-54S Histochemical study using lectins to identify glycoconjugates present in the efferent ducts and ductus epididymidis of men without testicular or related disease. The epididymal principal cells showed positive reactions to SBA over the apical microvilli but not in the cytoplasm. The reaction was observed in the caput and corpus epididymidis but not in the cauda. Positive reactions to SBA were also detected in the epididymal fluid and in the cytoplasm of mitochondria-rich cells (a minor population of epididymal epithelial cells). See: J Reprod Fertil 1996 Mar;106(2):313-20
N-acetylgalactosamine (GalNAc)-specific lectins, Dolichos biflorus agglutinin (DBA), and soybean agglutinin (SBA), enhanced Hantaan (HTN) virus infections in Vero E6 and P388D1 cells. See: Arch Virol 1999;144(9):1765-77 SBA is of vast importance to the field of clinical bone marrow transplantation and has been used to fractionate bone marrow cells. It binds bone marrow mononuclear cells, including mature myeloid, erythroid, and lymphoid cells, but has very low binding affinity and no toxic effect to the human hematopoietic cells. See: Mol Biotechnol 1999 Apr;11(2):181-94 For an opposing viewpoint, see: Am J Clin Oncol 1997 Aug;20(4):419-23
In human pancreas, soybean agglutinin (SBA) conjugated to horseradish peroxidase reacted with the acinar cells secreting blood group A and/or H antigen, but not with those secreting only B antigen. See: Glycine max agglutinin only reacted with hog mucin that is group A. See: Biochim Biophys Acta 2001 Feb 16;1525(1-2):50-7 Although under most normal circumstance SBA will bind with most human erythrocytes, it is classed, along with Codium fragile subspecies tomentosoides (CFT) Vicia villosa-A4 (VVL-A4), and Wistaria floribunda (WFL) lectins as a lectin specific for the blood group A specific disaccharide. See: Indian J Biochem Biophys 1997 Feb-Apr;34(1-2):61-71
In a test of the ability of a panel 30 lectins to bind with human respiratory epithelium, Soy bean agglutinin (SBA), and Dolichos biflorus agglutinin (DBA) were found to bind specifically to the tissue of blood group A and AB subjects. See: Microsc Res Tech 1997 Sep 1;38(5):505-11 Soybean lectin stimulates pancreatic exocrine secretion via CCK-A receptors in rats. See: Am J Physiol 1996 Apr;270(4 Pt 1):G653-9 SBA may be the cause of soy protein-induced damage of small bowel mucosa in infants. See: J Pediatr Gastroenterol Nutr 1983 May;2(2):271-87 SBA shows differential binding patterns with tissue sections of normal, hyperplastic and lactating human breast. See: J Pathol 1984 Apr;142(4):279-91
Aberrant pattern of lectin binding in low and high grade prostatic intraepithelial neoplasia: staining for soy bean agglutinin and Ulex europaeus agglutinin was negative in benign and hyperplastic glands and positive in dysplastic glands and carcinoma. See: Cancer 1995 May 15;75(10):2539-44 The loss of SBA lectin reactivity from human endometrium is a feature of malignant change. See: Pathol Res Pract 1996 Oct;192(10):989-97 Soybean agglutinin binds commonly to a subpopulation of small-diameter neurons in dorsal root ganglion, vascular endothelium and microglia in human spinal cord. See: Neurosci Lett 1992 Aug 17;142(2):131-4
Changes in the intestinal microvillus membrane (MVM) glycoproteins shown by lectin binding appear to be part of a complex postnatal maturational process in rats, involving different biochemical, functional, and biophysical membrane characteristics. See: Biol Neonate 1990;58(2):112-9
Human B-cell chronic lymphocytic leukaemia (B-CLL) cells showed the considerably lower ability to bind SBA and slightly higher expression of PNA and LEN receptors in comparison to normal B cells. See: Folia Haematol Int Mag Klin Morphol Blutforsch 1990;117(1):31-5 Soya lectin agglutinates both mesophyll and epidermal protoplasts from barleyand also interacts in a hapten-inhibitable fashion with components of soya bean protein body membrane. See: Canad J Botany 1994(72); 1688-1691 and Biolog Chem Hoppe-Seyler 1994 (375); 829-832 Soya agglutinin reacts preferentially with some rumen fungi . See: J Appl Bacteriol 1993 (74);29-35 Soya bean lectin agglutinates red cells from humans and several animal species. It also precipitates human A, blood group substances but reacts poorly with A2 and B substances and not at all with H substances. See: carbohydrate Res 1974 (37);89-112
Reaction with red cells and mitogenic activity towards neuraminidase-treated human and mouse lymphocytes is highly promoted by chemical or physical polymerisation. See: Biochem Biophys Res Comm 1973 (55);1347-1355 Soya agglutinin in the diet reduces the growth rate of young monogastric animals and induces dose- and polyamine-dependent and reversible hyperplastic growth of the small intestine and pancreatic hypertrophy. See: J Sci Food Agricul 1986 (37);1001-1010 and Digestion 1990 (46); 308-316 The lectin in the duodenal lumen stimulates pancreatic secretion via pancreatic cholecystokinin-A receptors and interferes with the absorption of Fe2+. See: Med Sci Res 1987 (15);1197-1198 and Amer J Physiol 1996 (33); 1190-1196 Parenteral administration of the soya lectin modulates the host's immune response and inhibits tumor growth. See: Chemotherapy 1994 (40); 272-278 The lectin is capable of differentiating between T-cells and stem cells of bone marrow. See: Lancet 1981 (2);327-331 Moreover, natural spleen suppressor cells and cyclophosphamide-generated suppressor cells react preferentially with soya lectin and can therefore be selectively isolated from bone marrow by agglutination. See: J. Leukocyte Biol 1992 (51);649-656
N-acetyl galactosamine. There is a slight preference for the alpha-anomeric over the beta-glycosidic linkage. It also reacts with galactose and its derivatives, but with less affinity.
For characterization of N-glycans, see: J Biochem (Tokyo). 1999 Jul;126(1):212-7 For characterization of root lectin, see: J Biol Chem. 1981 Dec 25;256(24):12905-10.
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