Relevant bibliographies by topics / Soybean Agglutinin (SBA)

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Academic literature on the topic 'Soybean Agglutinin (SBA)'

Author: Grafiati
Published: 6 September 2023
Last updated: 31 July 2025

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Journal articles on the topic "Soybean Agglutinin (SBA)"

1

Eguchi, M., T. Ozawa, J. Suda, K. Sugita, and T. Furukawa. "Lectins for electron microscopic distinction of eosinophils from other blood cells." Journal of Histochemistry & Cytochemistry 37, no. 5 (1989): 743–49. http://dx.doi.org/10.1177/37.5.2703708.

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Colloidal gold-labeled soybean agglutinin (SBA), Helix pomatia agglutinin (HPA), Dolichos biflorus agglutinin (DBA), and Griffonia simplicifolia lectin (GS-1) were used for electron microscopic observation of blood cells. Colloidal gold-labeled SBA, HPA, and DBA showed marked deposition on eosinophil granules at all stages of maturation. Gold particles were not deposited on basophils, neutrophils, monocytes, lymphocytes, or other blood cells. Only a few colloidal gold-labeled GS-1 were deposited on eosinophil granules. Eosinophil granules are rich in N-acetyl-D-galactosamine compounds, and the
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2

Abrosimov, Yu Yu. "FEATURES OF DISTRIBUTION OF SOYBEAN AGGLUTININ (SBA) RECEPTORS IN THE EXTRACELLULAR MATRIX OF THE MENISCI OF RAT KNEE JOINT AFTER INTRAFETAL INJECTION OF ANTIGENS." Biological Markers in Fundamental and Clinical Medicine (collection of abstracts) 3, no. 1 (2019): 61–63. http://dx.doi.org/10.29256/v.03.01.2019.escbm40.

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3

Ebell, W., H. Castro-Malaspina, MA Moore, and RJ O'Reilly. "Depletion of stromal cell elements in human marrow grafts separated by soybean agglutinin." Blood 65, no. 5 (1985): 1105–11. http://dx.doi.org/10.1182/blood.v65.5.1105.bloodjournal6551105.

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We report studies demonstrating the presence on human marrow stromal cells of binding sites for the soybean lectin (SBA). Marrow cells were separated by agglutination with SBA into an agglutinated cell (SBA+) fraction containing most mature hemic cells including T lymphocytes, and an unagglutinated cell (SBA-) fraction containing the hematopoietic stem cells. The vast majority of fibroblast colony-forming units (CFU- F) (97.2% +/- 1.1%) were in the SBA+ fraction. Mixing experiments using SBA+ and SBA- cells excluded the possibility that these results were caused by an unequal distribution of a
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4

Ebell, W., H. Castro-Malaspina, MA Moore, and RJ O'Reilly. "Depletion of stromal cell elements in human marrow grafts separated by soybean agglutinin." Blood 65, no. 5 (1985): 1105–11. http://dx.doi.org/10.1182/blood.v65.5.1105.1105.

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Abstract We report studies demonstrating the presence on human marrow stromal cells of binding sites for the soybean lectin (SBA). Marrow cells were separated by agglutination with SBA into an agglutinated cell (SBA+) fraction containing most mature hemic cells including T lymphocytes, and an unagglutinated cell (SBA-) fraction containing the hematopoietic stem cells. The vast majority of fibroblast colony-forming units (CFU- F) (97.2% +/- 1.1%) were in the SBA+ fraction. Mixing experiments using SBA+ and SBA- cells excluded the possibility that these results were caused by an unequal distribu
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5

Ito, N., K. Nishi, M. Nakajima, et al. "Histochemical reactivity of soybean agglutinin with blood group antigens and their precursor substances in acinar cells of human pancreas." Journal of Histochemistry & Cytochemistry 35, no. 8 (1987): 881–90. http://dx.doi.org/10.1177/35.8.2955034.

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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. For detailed histochemical characterization of SBA staining, the effects of treatment with unlabeled lectins and of digestion of certain enzymes on SBA staining were investigated in formalin-fixed, paraffin-embedded pancreatic tissue from individuals of different blood groups. Pre-incubation of sections with unlabeled Dolichos biflorus agglutinin to block A antigen eliminated subsequent SBA staining
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6

Sawyer, J. T., and R. A. Akeson. "Differential redistribution of lectin receptor classes on clonal rat myotubes and myoblasts." Journal of Cell Science 83, no. 1 (1986): 181–96. http://dx.doi.org/10.1242/jcs.83.1.181.

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To evaluate the relative mobilities of cell surface glycoconjugates during myogenesis we have studied the redistribution of fluorescein-conjugated plant lectins on L6 rat myogenic cells. Previous experiments had demonstrated that the receptors for the lectins soybean agglutinin (SBA), wheat germ agglutinin, concanavalin A and Lens culinaris agglutinin all were relatively uniformly distributed on both myoblasts and myotubes, and that SBA receptors were capable of rapid redistribution on myotubes but not myoblasts at 4 degrees C (Sawyer & Akeson, 1983). Here we show that when SBA-labelled my
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7

Zhang, Menghan, Yulou Qiu, Ajuan You, et al. "Development of a Phage-Displayed Nanobody-Based Competitive Immunoassay for the Sensitive Detection of Soybean Agglutinin." Foods 13, no. 12 (2024): 1893. http://dx.doi.org/10.3390/foods13121893.

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Soybean agglutinin (SBA) is a primary antinutritional factor in soybeans that can inhibit the growth of humans and mammals, disrupt the intestinal environment, and cause pathological changes. Therefore, detecting and monitoring SBA in foods is essential for safeguarding human health. In this paper, M13 phage-displayed nanobodies against SBA were isolated from a naive nanobody library. An M13 phage-displayed nanobody-based competitive enzyme-linked immunosorbent assay (P-cELISA) was then established for SBA analysis using biotinylated anti-M13 phage antibody (biotin-anti-M13) and streptavidin p
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8

Suzaki, E., and K. Kataoka. "Lectin cytochemistry in the gastrointestinal tract with special reference to glycosylation in the Golgi apparatus of Brunner's gland cells." Journal of Histochemistry & Cytochemistry 40, no. 3 (1992): 379–85. http://dx.doi.org/10.1177/40.3.1552177.

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Two hydrophilic, low temperature-embedding resins, Lowicryl K4M and LR White, were compared in lectin cytochemistry. Post-embedding staining of colloidal gold-labeled Griffonia symplicifolia agglutinin II (GSA-II) resulted in staining of the Golgi apparatus and mucous granules of mucous neck cells in the gastric fundic gland, pylorocytes, and Brunner's gland cells embedded in either resin, although it was much easier to make ultra-thin sections with LR White-embedded material than with the other. Post-fixation with uranyl acetate followed by LR White embedding improved general ultrastructure s
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9

Gallagher, Betty C. "Basal laminar thinning in branching morphogenesis of the chick lung as demonstrated by lectin probes." Development 94, no. 1 (1986): 173–88. http://dx.doi.org/10.1242/dev.94.1.173.

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Three lectins, wheat germ agglutinin (WGA), soybean agglutinin (SBA) and Ricinis communis agglutinin I (RCA), were used to study the basement membrane of developing chick lungs. Thinning of the basement membrane at the tips of newly formed bronchi was visualized with all three lectins, but was particularly evident using SBA. Control sections established the ability of the lectins to stain hyaluronic acid and chondroitin sulphate. Neuraminidase, bovine testes hyaluronidase and Streptomyces hyaluronidase removed some of the staining, but none were able to affect the staining of the basement memb
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10

Swamy, Musti Joginadha, and Avadhesha Surolia. "Studies on the tryptophan residues of soybean agglutinin. Involvement in saccharide binding." Bioscience Reports 9, no. 2 (1989): 189–98. http://dx.doi.org/10.1007/bf01115995.

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Modification of tryptophan side chains of soybean agglutinin (SBA) with N-bromosuccinimide results in a loss of the hemagglutinating and carbohydrate binding activities of the protein. One residue/subunit is probably essential for the binding activity. Modification leads to a large decrease in the fluorescene of the protein accompained by a blue shift. Iodide ion quenching of the protein fluorescence shows that saccharide binding results in a decreased accessibility of some of the tryptophan side chains. These results strongly point towards the involvement of tryptophan residues in the active
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Dissertations / Theses on the topic "Soybean Agglutinin (SBA)"

1

Sinha, Sharmistha. "Role of Glycosylation and Oligomerization on the Stability of Soybean Agglutinin." Thesis, 2006. https://etd.iisc.ac.in/handle/2005/4988.

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Carbohydrates are vital to life. In their naive form, they serve as a primary energy source for supporting life. However, in most cases carbohydrates do not exist as simple sugars in nature. Instead they occur as more complex molecular conjugates known as the glycans and Glycobiology is the study of the roles of these glycans in various biological events. The study of sugars is gaining importance in all strata of today’s scientific world, be it cell biology, immunology or even neurobiology. These glycans do not exist at the cell surface or in the extracellular matrix as free-standing polymers.
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