binding saturation isotherm Search Results


saturation binding isotherm  (GraphPad Software Inc)
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GraphPad Software Inc saturation binding isotherm
Competitive inhibition of gp120-CD4 binding by BMS-378806 and binding affinity of BMS-378806 to gp120. (A) <t>Saturation</t> binding curve of BMS-378806. The levels of sCD4 bound to gp120 in the absence or presence of various concentrations of BMS-378806 and in escalating concentrations of sCD4 were measured by using the gp120-CD4 binding ELISA. BMS-378806 concentrations: ▪, 0 μM; ▴, 0.8 μM; ▾, 1.6 μM; ⧫, 3.2 μM. Data were analyzed according to the one-site binding model with GraphPad Prism. OD450, optical density at 450 nm. (B) Apparent binding constants for sCD4 in the absence and presence of BMS-378806. The Kd and Bmax values were derived by using nonlinear regression analysis with GraphPad Prism. Values were the means ± standard errors of the means, representing two independent experiments. (C) Binding affinity of BMS-378806 to gp120 by SPA. [3H]BMS-378806 binding to the gp120 protein was measured by employing gp120-coated SPA beads. The amount of gp120-bound [3H]BMS-378806 was determined by using a Packard TopCount scintillation counter. The results from Scatchard analysis of binding isotherm are shown in the insert. The x axis represents bound (corrected), and the y axis indicates bound/free.
Saturation Binding Isotherm, supplied by GraphPad Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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binding isotherm or saturation binding curve originpro 8g sr2  (OriginLab corp)
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OriginLab corp binding isotherm or saturation binding curve originpro 8g sr2
Affinity tests on the representatives of aptamer groups evolved from Capture-SELEX. Affinity tests were performed similar to the Capture-SELEX procedure, and ssDNA was eluted by different concentrations of kanamycin A in selection buffer. Data was fitted by the model of one site direct binding using a rectangular hyperbola for the saturation curve (OriginLab Corporation, <t>OriginPro</t> <t>8G</t> <t>SR2).</t>
Binding Isotherm Or Saturation Binding Curve Originpro 8g Sr2, supplied by OriginLab corp, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Competitive inhibition of gp120-CD4 binding by BMS-378806 and binding affinity of BMS-378806 to gp120. (A) Saturation binding curve of BMS-378806. The levels of sCD4 bound to gp120 in the absence or presence of various concentrations of BMS-378806 and in escalating concentrations of sCD4 were measured by using the gp120-CD4 binding ELISA. BMS-378806 concentrations: ▪, 0 μM; ▴, 0.8 μM; ▾, 1.6 μM; ⧫, 3.2 μM. Data were analyzed according to the one-site binding model with GraphPad Prism. OD450, optical density at 450 nm. (B) Apparent binding constants for sCD4 in the absence and presence of BMS-378806. The Kd and Bmax values were derived by using nonlinear regression analysis with GraphPad Prism. Values were the means ± standard errors of the means, representing two independent experiments. (C) Binding affinity of BMS-378806 to gp120 by SPA. [3H]BMS-378806 binding to the gp120 protein was measured by employing gp120-coated SPA beads. The amount of gp120-bound [3H]BMS-378806 was determined by using a Packard TopCount scintillation counter. The results from Scatchard analysis of binding isotherm are shown in the insert. The x axis represents bound (corrected), and the y axis indicates bound/free.

Journal:

Article Title: Biochemical and Genetic Characterizations of a Novel Human Immunodeficiency Virus Type 1 Inhibitor That Blocks gp120-CD4 Interactions

doi: 10.1128/JVI.77.19.10528-10536.2003

Figure Lengend Snippet: Competitive inhibition of gp120-CD4 binding by BMS-378806 and binding affinity of BMS-378806 to gp120. (A) Saturation binding curve of BMS-378806. The levels of sCD4 bound to gp120 in the absence or presence of various concentrations of BMS-378806 and in escalating concentrations of sCD4 were measured by using the gp120-CD4 binding ELISA. BMS-378806 concentrations: ▪, 0 μM; ▴, 0.8 μM; ▾, 1.6 μM; ⧫, 3.2 μM. Data were analyzed according to the one-site binding model with GraphPad Prism. OD450, optical density at 450 nm. (B) Apparent binding constants for sCD4 in the absence and presence of BMS-378806. The Kd and Bmax values were derived by using nonlinear regression analysis with GraphPad Prism. Values were the means ± standard errors of the means, representing two independent experiments. (C) Binding affinity of BMS-378806 to gp120 by SPA. [3H]BMS-378806 binding to the gp120 protein was measured by employing gp120-coated SPA beads. The amount of gp120-bound [3H]BMS-378806 was determined by using a Packard TopCount scintillation counter. The results from Scatchard analysis of binding isotherm are shown in the insert. The x axis represents bound (corrected), and the y axis indicates bound/free.

Article Snippet: The curve represents the best fit to a saturation binding isotherm determined by using GraphPad Prism.

Techniques: Inhibition, Binding Assay, Enzyme-linked Immunosorbent Assay, Derivative Assay

Binding stoichiometry of BMS-378806 to gp120 protein. gp120JRFL (1.0 μM) was titrated with BMS-378806, and the observed percent reduction in fluorescence from each of four independent experiments was plotted first as a function of BMS-378806 concentration (data not shown). Each of these data sets was then normalized to the percent maximal fluorescence reduction observed for each experiment in order to analyze the four sets of data together. The individual, normalized data sets are depicted as open squares, closed squares, closed diamonds, and open triangles. The curve represents the best fit to a saturation binding isotherm determined by using GraphPad Prism.

Journal:

Article Title: Biochemical and Genetic Characterizations of a Novel Human Immunodeficiency Virus Type 1 Inhibitor That Blocks gp120-CD4 Interactions

doi: 10.1128/JVI.77.19.10528-10536.2003

Figure Lengend Snippet: Binding stoichiometry of BMS-378806 to gp120 protein. gp120JRFL (1.0 μM) was titrated with BMS-378806, and the observed percent reduction in fluorescence from each of four independent experiments was plotted first as a function of BMS-378806 concentration (data not shown). Each of these data sets was then normalized to the percent maximal fluorescence reduction observed for each experiment in order to analyze the four sets of data together. The individual, normalized data sets are depicted as open squares, closed squares, closed diamonds, and open triangles. The curve represents the best fit to a saturation binding isotherm determined by using GraphPad Prism.

Article Snippet: The curve represents the best fit to a saturation binding isotherm determined by using GraphPad Prism.

Techniques: Binding Assay, Fluorescence, Concentration Assay

Affinity tests on the representatives of aptamer groups evolved from Capture-SELEX. Affinity tests were performed similar to the Capture-SELEX procedure, and ssDNA was eluted by different concentrations of kanamycin A in selection buffer. Data was fitted by the model of one site direct binding using a rectangular hyperbola for the saturation curve (OriginLab Corporation, OriginPro 8G SR2).

Journal: Journal of Analytical Methods in Chemistry

Article Title: Capture-SELEX: Selection of DNA Aptamers for Aminoglycoside Antibiotics

doi: 10.1155/2012/415697

Figure Lengend Snippet: Affinity tests on the representatives of aptamer groups evolved from Capture-SELEX. Affinity tests were performed similar to the Capture-SELEX procedure, and ssDNA was eluted by different concentrations of kanamycin A in selection buffer. Data was fitted by the model of one site direct binding using a rectangular hyperbola for the saturation curve (OriginLab Corporation, OriginPro 8G SR2).

Article Snippet: These amounts are then quantified by fluorescence detection , and the resulting data is fitted by the model of one-site direct binding using a rectangular hyperbola also known as binding isotherm or saturation binding curve (OriginLab Corproration, OriginPro 8G SR2).

Techniques: Selection, Binding Assay