ArticleCell biochemistry and biophysics2026
Kinetic and Apparent Thermodynamic Analysis of Phaseolus Vulgaris Leucoagglutinin Binding to Cell-Surface Glycans in SR Lymphoma Cells Using a Fixation-Modified Cell-ELISA.
Article in Cell biochemistry and biophysics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Cell-surface glycosylation plays an important role in lectin-mediated molecular recognition and is frequently altered in malignant cells. In this study, a fixation-modified cell-ELISA was developed to enable stable immobilization of non-adherent cells and to compare the binding behavior of Phaseolus vulgaris leucoagglutinin (PHA-L) toward SR lymphoma cells and normal human peripheral blood mononuclear cells (PBMCs). Saturation binding and time-course assays were performed at 5, 15, 25, and 37 °C, and the resulting whole-cell ELISA data were analyzed using Langmuir, Van't Hoff, Arrhenius, and Eyring models to obtain comparative apparent kinetic and thermodynamic descriptors. Saturation binding analysis showed lower apparent equilibrium dissociation constants (Kd
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