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enzyme kinetics mixed model inhibition curve fitting algorithm  (GraphPad Software Inc)

 
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    Structured Review

    GraphPad Software Inc enzyme kinetics mixed model inhibition curve fitting algorithm
    Structures of the compounds are shown in Panels A-C: A, Flu-AM1; B, Ibu-AM5; C, ibufenac-AM1. The asterisks show the chiral centres. In Panels D-F, the <t>inhibition</t> of 0.5 μM [ 3 H]AEA hydrolysis in rat brain homogenates by the compounds is shown. Data are means ± SEM (when not enclosed by the symbols), N = 3 for the enantiomers of D, Flu-AM1; E, Ibu-AM5 and F, racemic Ibu-AM5 and Ibufenac-AM1.
    Enzyme Kinetics Mixed Model Inhibition Curve Fitting Algorithm, 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
    https://www.bioz.com/result/enzyme kinetics mixed model inhibition curve fitting algorithm/product/GraphPad Software Inc
    Average 90 stars, based on 1 article reviews
    enzyme kinetics mixed model inhibition curve fitting algorithm - by Bioz Stars, 2026-03
    90/100 stars

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    1) Product Images from "Interaction of the N -(3-Methylpyridin-2-yl)amide Derivatives of Flurbiprofen and Ibuprofen with FAAH: Enantiomeric Selectivity and Binding Mode"

    Article Title: Interaction of the N -(3-Methylpyridin-2-yl)amide Derivatives of Flurbiprofen and Ibuprofen with FAAH: Enantiomeric Selectivity and Binding Mode

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0142711

    Structures of the compounds are shown in Panels A-C: A, Flu-AM1; B, Ibu-AM5; C, ibufenac-AM1. The asterisks show the chiral centres. In Panels D-F, the inhibition of 0.5 μM [ 3 H]AEA hydrolysis in rat brain homogenates by the compounds is shown. Data are means ± SEM (when not enclosed by the symbols), N = 3 for the enantiomers of D, Flu-AM1; E, Ibu-AM5 and F, racemic Ibu-AM5 and Ibufenac-AM1.
    Figure Legend Snippet: Structures of the compounds are shown in Panels A-C: A, Flu-AM1; B, Ibu-AM5; C, ibufenac-AM1. The asterisks show the chiral centres. In Panels D-F, the inhibition of 0.5 μM [ 3 H]AEA hydrolysis in rat brain homogenates by the compounds is shown. Data are means ± SEM (when not enclosed by the symbols), N = 3 for the enantiomers of D, Flu-AM1; E, Ibu-AM5 and F, racemic Ibu-AM5 and Ibufenac-AM1.

    Techniques Used: Inhibition

    Species-dependent inhibition of FAAH by the enantiomers of Flu-AM1 and Ibu-AM5.
    Figure Legend Snippet: Species-dependent inhibition of FAAH by the enantiomers of Flu-AM1 and Ibu-AM5.

    Techniques Used: Inhibition

    Panels A and B show the time-dependencies of ( R )-Flu-AM1 and URB597, respectively. The data are means ± SEM, N = 3. In Panel C, homogenates (at 20-fold normal strength) were preincubated with either vehicle, 2, 4 or 6 μM ( R )-Flu-AM1 for 60 min. Aliquots were then diluted 20-fold and assayed for FAAH activity. These are shown as 2 →0.1, 4 →0.2 and 6 →0.3. Concomitantly, ( R )-Flu-AM1 was added to vehicle-preincubated aliquots to give concentrations of 0.1, 0.2 and 0.3 μM (representing free concentrations after a 20- fold dilution), 2, 4 and 6 μM final concentrations. The panel shows the data as % of corresponding control (means ± SEM, N = 3). For a fully reversible compound, the inhibition seen in the yellow bars (i.e. following the dilution) should be lower than in the purple bars (the inhibition seen at the undiluted concentrations) but equal to the green bars (the free concentrations after the dilution).
    Figure Legend Snippet: Panels A and B show the time-dependencies of ( R )-Flu-AM1 and URB597, respectively. The data are means ± SEM, N = 3. In Panel C, homogenates (at 20-fold normal strength) were preincubated with either vehicle, 2, 4 or 6 μM ( R )-Flu-AM1 for 60 min. Aliquots were then diluted 20-fold and assayed for FAAH activity. These are shown as 2 →0.1, 4 →0.2 and 6 →0.3. Concomitantly, ( R )-Flu-AM1 was added to vehicle-preincubated aliquots to give concentrations of 0.1, 0.2 and 0.3 μM (representing free concentrations after a 20- fold dilution), 2, 4 and 6 μM final concentrations. The panel shows the data as % of corresponding control (means ± SEM, N = 3). For a fully reversible compound, the inhibition seen in the yellow bars (i.e. following the dilution) should be lower than in the purple bars (the inhibition seen at the undiluted concentrations) but equal to the green bars (the free concentrations after the dilution).

    Techniques Used: Activity Assay, Control, Inhibition

    ( R )-Flu-AM1 and B. carprofen. Samples were incubated for 18 h with inhibitor and substrate (0.5 μM [ 3 H]AEA). The concentrations of lysates used were FAAH wt , 0.04 μg/assay, FAAH T488A , 0.4 μg/assay, empty vector 0.36 μg/assay. Shown are means ± SEM, N = 3–6. The pI 50 values, with corresponding IC 50 and n H values in brackets were: ( R )-Flu-AM1: FAAH wt , 5.08±0.03 (8.3 μM; n H = 1.02±0.07); FAAH T488A , 4.55±0.07 (28 μM; n H = 1.47±0.37), FAAH wt + empty vector, 5.10±0.02 (8.0 μM; n H = 0.99±0.06). Carprofen: FAAH wt , 4.43±0.02 (37 μM, n H = 3.00±0.31); FAAH T488A , 4.32±0.04 (48 μM, n H = 2.43±0.37), FAAH wt + empty vector, 4.50±0.01 (32 μM; n H = 4.28±0.41. Note that for carprofen and wild-type FAAH, the analyses suggested that a curve with a maximum inhibition of 82–91% fitted the data better than a curve with 100% maximum inhibition, and these values have been used here.
    Figure Legend Snippet: ( R )-Flu-AM1 and B. carprofen. Samples were incubated for 18 h with inhibitor and substrate (0.5 μM [ 3 H]AEA). The concentrations of lysates used were FAAH wt , 0.04 μg/assay, FAAH T488A , 0.4 μg/assay, empty vector 0.36 μg/assay. Shown are means ± SEM, N = 3–6. The pI 50 values, with corresponding IC 50 and n H values in brackets were: ( R )-Flu-AM1: FAAH wt , 5.08±0.03 (8.3 μM; n H = 1.02±0.07); FAAH T488A , 4.55±0.07 (28 μM; n H = 1.47±0.37), FAAH wt + empty vector, 5.10±0.02 (8.0 μM; n H = 0.99±0.06). Carprofen: FAAH wt , 4.43±0.02 (37 μM, n H = 3.00±0.31); FAAH T488A , 4.32±0.04 (48 μM, n H = 2.43±0.37), FAAH wt + empty vector, 4.50±0.01 (32 μM; n H = 4.28±0.41. Note that for carprofen and wild-type FAAH, the analyses suggested that a curve with a maximum inhibition of 82–91% fitted the data better than a curve with 100% maximum inhibition, and these values have been used here.

    Techniques Used: Incubation, Plasmid Preparation, Inhibition



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    enzyme kinetics mixed model inhibition curve fitting algorithm  (GraphPad Software Inc)
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    GraphPad Software Inc enzyme kinetics mixed model inhibition curve fitting algorithm
    Structures of the compounds are shown in Panels A-C: A, Flu-AM1; B, Ibu-AM5; C, ibufenac-AM1. The asterisks show the chiral centres. In Panels D-F, the <t>inhibition</t> of 0.5 μM [ 3 H]AEA hydrolysis in rat brain homogenates by the compounds is shown. Data are means ± SEM (when not enclosed by the symbols), N = 3 for the enantiomers of D, Flu-AM1; E, Ibu-AM5 and F, racemic Ibu-AM5 and Ibufenac-AM1.
    Enzyme Kinetics Mixed Model Inhibition Curve Fitting Algorithm, 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
    https://www.bioz.com/result/enzyme kinetics mixed model inhibition curve fitting algorithm/product/GraphPad Software Inc
    Average 90 stars, based on 1 article reviews
    enzyme kinetics mixed model inhibition curve fitting algorithm - by Bioz Stars, 2026-03
    90/100 stars
    		  Buy from Supplier

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    Structures of the compounds are shown in Panels A-C: A, Flu-AM1; B, Ibu-AM5; C, ibufenac-AM1. The asterisks show the chiral centres. In Panels D-F, the inhibition of 0.5 μM [ 3 H]AEA hydrolysis in rat brain homogenates by the compounds is shown. Data are means ± SEM (when not enclosed by the symbols), N = 3 for the enantiomers of D, Flu-AM1; E, Ibu-AM5 and F, racemic Ibu-AM5 and Ibufenac-AM1.

    Journal: PLoS ONE

    Article Title: Interaction of the N -(3-Methylpyridin-2-yl)amide Derivatives of Flurbiprofen and Ibuprofen with FAAH: Enantiomeric Selectivity and Binding Mode

    doi: 10.1371/journal.pone.0142711

    Figure Lengend Snippet: Structures of the compounds are shown in Panels A-C: A, Flu-AM1; B, Ibu-AM5; C, ibufenac-AM1. The asterisks show the chiral centres. In Panels D-F, the inhibition of 0.5 μM [ 3 H]AEA hydrolysis in rat brain homogenates by the compounds is shown. Data are means ± SEM (when not enclosed by the symbols), N = 3 for the enantiomers of D, Flu-AM1; E, Ibu-AM5 and F, racemic Ibu-AM5 and Ibufenac-AM1.

    Article Snippet: K i and α values were obtained using the enzyme kinetics mixed model inhibition curve fitting algorithm available in the GraphPad Prism programme.

    Techniques: Inhibition

    Species-dependent inhibition of FAAH by the enantiomers of Flu-AM1 and Ibu-AM5.

    Journal: PLoS ONE

    Article Title: Interaction of the N -(3-Methylpyridin-2-yl)amide Derivatives of Flurbiprofen and Ibuprofen with FAAH: Enantiomeric Selectivity and Binding Mode

    doi: 10.1371/journal.pone.0142711

    Figure Lengend Snippet: Species-dependent inhibition of FAAH by the enantiomers of Flu-AM1 and Ibu-AM5.

    Article Snippet: K i and α values were obtained using the enzyme kinetics mixed model inhibition curve fitting algorithm available in the GraphPad Prism programme.

    Techniques: Inhibition

    Panels A and B show the time-dependencies of ( R )-Flu-AM1 and URB597, respectively. The data are means ± SEM, N = 3. In Panel C, homogenates (at 20-fold normal strength) were preincubated with either vehicle, 2, 4 or 6 μM ( R )-Flu-AM1 for 60 min. Aliquots were then diluted 20-fold and assayed for FAAH activity. These are shown as 2 →0.1, 4 →0.2 and 6 →0.3. Concomitantly, ( R )-Flu-AM1 was added to vehicle-preincubated aliquots to give concentrations of 0.1, 0.2 and 0.3 μM (representing free concentrations after a 20- fold dilution), 2, 4 and 6 μM final concentrations. The panel shows the data as % of corresponding control (means ± SEM, N = 3). For a fully reversible compound, the inhibition seen in the yellow bars (i.e. following the dilution) should be lower than in the purple bars (the inhibition seen at the undiluted concentrations) but equal to the green bars (the free concentrations after the dilution).

    Journal: PLoS ONE

    Article Title: Interaction of the N -(3-Methylpyridin-2-yl)amide Derivatives of Flurbiprofen and Ibuprofen with FAAH: Enantiomeric Selectivity and Binding Mode

    doi: 10.1371/journal.pone.0142711

    Figure Lengend Snippet: Panels A and B show the time-dependencies of ( R )-Flu-AM1 and URB597, respectively. The data are means ± SEM, N = 3. In Panel C, homogenates (at 20-fold normal strength) were preincubated with either vehicle, 2, 4 or 6 μM ( R )-Flu-AM1 for 60 min. Aliquots were then diluted 20-fold and assayed for FAAH activity. These are shown as 2 →0.1, 4 →0.2 and 6 →0.3. Concomitantly, ( R )-Flu-AM1 was added to vehicle-preincubated aliquots to give concentrations of 0.1, 0.2 and 0.3 μM (representing free concentrations after a 20- fold dilution), 2, 4 and 6 μM final concentrations. The panel shows the data as % of corresponding control (means ± SEM, N = 3). For a fully reversible compound, the inhibition seen in the yellow bars (i.e. following the dilution) should be lower than in the purple bars (the inhibition seen at the undiluted concentrations) but equal to the green bars (the free concentrations after the dilution).

    Article Snippet: K i and α values were obtained using the enzyme kinetics mixed model inhibition curve fitting algorithm available in the GraphPad Prism programme.

    Techniques: Activity Assay, Control, Inhibition

    ( R )-Flu-AM1 and B. carprofen. Samples were incubated for 18 h with inhibitor and substrate (0.5 μM [ 3 H]AEA). The concentrations of lysates used were FAAH wt , 0.04 μg/assay, FAAH T488A , 0.4 μg/assay, empty vector 0.36 μg/assay. Shown are means ± SEM, N = 3–6. The pI 50 values, with corresponding IC 50 and n H values in brackets were: ( R )-Flu-AM1: FAAH wt , 5.08±0.03 (8.3 μM; n H = 1.02±0.07); FAAH T488A , 4.55±0.07 (28 μM; n H = 1.47±0.37), FAAH wt + empty vector, 5.10±0.02 (8.0 μM; n H = 0.99±0.06). Carprofen: FAAH wt , 4.43±0.02 (37 μM, n H = 3.00±0.31); FAAH T488A , 4.32±0.04 (48 μM, n H = 2.43±0.37), FAAH wt + empty vector, 4.50±0.01 (32 μM; n H = 4.28±0.41. Note that for carprofen and wild-type FAAH, the analyses suggested that a curve with a maximum inhibition of 82–91% fitted the data better than a curve with 100% maximum inhibition, and these values have been used here.

    Journal: PLoS ONE

    Article Title: Interaction of the N -(3-Methylpyridin-2-yl)amide Derivatives of Flurbiprofen and Ibuprofen with FAAH: Enantiomeric Selectivity and Binding Mode

    doi: 10.1371/journal.pone.0142711

    Figure Lengend Snippet: ( R )-Flu-AM1 and B. carprofen. Samples were incubated for 18 h with inhibitor and substrate (0.5 μM [ 3 H]AEA). The concentrations of lysates used were FAAH wt , 0.04 μg/assay, FAAH T488A , 0.4 μg/assay, empty vector 0.36 μg/assay. Shown are means ± SEM, N = 3–6. The pI 50 values, with corresponding IC 50 and n H values in brackets were: ( R )-Flu-AM1: FAAH wt , 5.08±0.03 (8.3 μM; n H = 1.02±0.07); FAAH T488A , 4.55±0.07 (28 μM; n H = 1.47±0.37), FAAH wt + empty vector, 5.10±0.02 (8.0 μM; n H = 0.99±0.06). Carprofen: FAAH wt , 4.43±0.02 (37 μM, n H = 3.00±0.31); FAAH T488A , 4.32±0.04 (48 μM, n H = 2.43±0.37), FAAH wt + empty vector, 4.50±0.01 (32 μM; n H = 4.28±0.41. Note that for carprofen and wild-type FAAH, the analyses suggested that a curve with a maximum inhibition of 82–91% fitted the data better than a curve with 100% maximum inhibition, and these values have been used here.

    Article Snippet: K i and α values were obtained using the enzyme kinetics mixed model inhibition curve fitting algorithm available in the GraphPad Prism programme.

    Techniques: Incubation, Plasmid Preparation, Inhibition